ANATOMY & PHYSIOLOGY OF THE NEURON ANATOMY & PHYSIOLOGY 2013-2014.
111008(Anatomy Physiology)
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Leslie Ann Labuga 11-11-08
BSN 1A
ANATOMY @ PHYSIOLOGY
Assignment: ORGANIC COMPOUND-THE BASIS OF LIFE
1. Differentiate carbohydrates, lipids, and proteins: give their basic structural attribution.
Answer;
Carbohydrates (from 'hydrates ofcarbon') or saccharides(Greek, skcharon, meaning"sugar") are the mostabundant of the four major classes ofbiomolecules. They fill numerous roles in living things, such as the storage and
transport ofenergy(starch, glycogen) and structural components (cellulose in plants, chitin in animals). Additionally,
carbohydrates and their derivatives play major roles in the working process of the immune system, fertilization,
pathogenesis, blood clotting, and development.
Chemically, carbohydrates are simple organic compounds that are aldehydes or ketoneswith manyhydroxyl groupsadded, usually one on each carbon atom that is not part of the aldehyde or ketone functional group. The basic
carbohydrate units are called monosaccharides, such as glucose, galactose, and fructose. The general stoichiometric
formulaof an unmodified monosaccharide is (CH2O)n, where n is any number of three or greater; however, the use of
this word does not follow this exact definition and many molecules with formulae that differ slightly from this are still
called carbohydrates, and others that possess formulae agreeing with this general rule are not called carbohydrates (eg
formaldehyde).
Monosaccharides can be linked together into what are called polysaccharides (or oligosaccharides) in almost limitless
ways. Many carbohydrates contain one or more modified monosaccharide units that have had one or more groups
replaced or removed. For example, deoxyribose, a component ofDNA, is a modified version ofribose; chitin is
composed of repeating units ofN-acetylglucosamine, anitrogen-containing form of glucose. The names of
carbohydrates often end in the suffix -ose.
*karbo-hi drat = organic compound compose of carbon, hydrogen, and oxygen includes; starch, sugars, cellulose.
Lipids are broadly defined as any fat-soluble (lipophilic), naturally-occurringmolecule, such as fats, oils, waxes,cholesterol, sterols, fat-soluble vitamins (such as vitamins A, D, E and K), monoglycerides, diglycerides, phospholipids,
and others. The main biological functions of lipids include energy storage, acting as structural components of cell
membranes, and participating as importantsignaling molecules.
Although the term lipidis sometimes used as a synonym for fats, fats are a subgroup of lipids called triglycerides and
should not be confused with the term fatty acid. Lipids also encompass molecules such as fatty acids and their
derivatives (includingtri-, di-, and monoglycerides and phospholipids), as well as other sterol-containingmetabolites
such as cholesterol.The emulsion testis a crude method for determining the presence or absence of lipids in a given
sample.
Lipids are a diverse group of compounds that have many key biological functions, such as structural components of
cell membranes, energy storage sources and intermediates in signaling pathways. Lipids may be broadly defined as
hydrophobic or amphiphilic small molecules that originate entirely or in part from two distinct types of biochemical
subunits or "building blocks": ketoacyl and isoprene groups. Using this approach, lipids may be divided into eight
categories : fatty acyls, glycerolipids, glycerophospholipids, sphingolipids, saccharolipids and polyketides (derived from
condensation of ketoacyl subunits); and sterol lipids and prenol lipids (derived from condensation of isoprene
subunits).
http://en.wikipedia.org/wiki/Hydratehttp://en.wikipedia.org/wiki/Carbonhttp://en.wikipedia.org/wiki/Greek_languagehttp://en.wikipedia.org/wiki/Sugarhttp://en.wikipedia.org/wiki/Biomoleculehttp://en.wikipedia.org/wiki/Energyhttp://en.wikipedia.org/wiki/Starchhttp://en.wikipedia.org/wiki/Glycogenhttp://en.wikipedia.org/wiki/Cellulosehttp://en.wikipedia.org/wiki/Chitinhttp://en.wikipedia.org/wiki/Immune_systemhttp://en.wikipedia.org/wiki/Fertilizationhttp://en.wikipedia.org/wiki/Pathogenesishttp://en.wikipedia.org/wiki/Blood_clottinghttp://en.wikipedia.org/wiki/Developmental_biologyhttp://en.wikipedia.org/wiki/Organic_compoundhttp://en.wikipedia.org/wiki/Aldehydehttp://en.wikipedia.org/wiki/Ketonehttp://en.wikipedia.org/wiki/Hydroxylhttp://en.wikipedia.org/wiki/Functional_grouphttp://en.wikipedia.org/wiki/Monosaccharidehttp://en.wikipedia.org/wiki/Glucosehttp://en.wikipedia.org/wiki/Galactosehttp://en.wikipedia.org/wiki/Fructosehttp://en.wikipedia.org/wiki/Stoichiometryhttp://en.wikipedia.org/wiki/Chemical_formulahttp://en.wikipedia.org/wiki/Polysaccharidehttp://en.wikipedia.org/wiki/Oligosaccharidehttp://en.wikipedia.org/wiki/Deoxyribosehttp://en.wikipedia.org/wiki/DNAhttp://en.wikipedia.org/wiki/Ribosehttp://en.wikipedia.org/wiki/Chitinhttp://en.wikipedia.org/wiki/N-acetylglucosaminehttp://en.wikipedia.org/wiki/Nitrogenhttp://en.wikipedia.org/wiki/-osehttp://en.wikipedia.org/wiki/Solublehttp://en.wikipedia.org/wiki/Lipophilicityhttp://en.wikipedia.org/wiki/Moleculehttp://en.wikipedia.org/wiki/Vitaminhttp://en.wikipedia.org/wiki/Monoglycerideshttp://en.wikipedia.org/wiki/Diglycerideshttp://en.wikipedia.org/wiki/Phospholipidshttp://en.wikipedia.org/wiki/Cell_membranehttp://en.wikipedia.org/wiki/Cell_membranehttp://en.wikipedia.org/wiki/Lipid_signalinghttp://en.wikipedia.org/wiki/Fathttp://en.wikipedia.org/wiki/Triglyceridehttp://en.wikipedia.org/wiki/Fatty_acidhttp://en.wikipedia.org/wiki/Triglyceridehttp://en.wikipedia.org/wiki/Diglyceridehttp://en.wikipedia.org/wiki/Monoglyceridehttp://en.wikipedia.org/wiki/Phospholipidhttp://en.wikipedia.org/wiki/Sterolhttp://en.wikipedia.org/wiki/Metabolitehttp://en.wikipedia.org/wiki/Cholesterolhttp://en.wikipedia.org/wiki/Emulsion_testhttp://en.wikipedia.org/wiki/Hydrophobehttp://en.wikipedia.org/wiki/Amphiphilehttp://en.wikipedia.org/wiki/Ketonehttp://en.wikipedia.org/wiki/Isoprenehttp://en.wikipedia.org/wiki/Isoprenehttp://en.wikipedia.org/wiki/Ketonehttp://en.wikipedia.org/wiki/Amphiphilehttp://en.wikipedia.org/wiki/Hydrophobehttp://en.wikipedia.org/wiki/Emulsion_testhttp://en.wikipedia.org/wiki/Cholesterolhttp://en.wikipedia.org/wiki/Metabolitehttp://en.wikipedia.org/wiki/Sterolhttp://en.wikipedia.org/wiki/Phospholipidhttp://en.wikipedia.org/wiki/Monoglyceridehttp://en.wikipedia.org/wiki/Diglyceridehttp://en.wikipedia.org/wiki/Triglyceridehttp://en.wikipedia.org/wiki/Fatty_acidhttp://en.wikipedia.org/wiki/Triglyceridehttp://en.wikipedia.org/wiki/Fathttp://en.wikipedia.org/wiki/Lipid_signalinghttp://en.wikipedia.org/wiki/Cell_membranehttp://en.wikipedia.org/wiki/Cell_membranehttp://en.wikipedia.org/wiki/Phospholipidshttp://en.wikipedia.org/wiki/Diglycerideshttp://en.wikipedia.org/wiki/Monoglycerideshttp://en.wikipedia.org/wiki/Vitaminhttp://en.wikipedia.org/wiki/Moleculehttp://en.wikipedia.org/wiki/Lipophilicityhttp://en.wikipedia.org/wiki/Solublehttp://en.wikipedia.org/wiki/-osehttp://en.wikipedia.org/wiki/Nitrogenhttp://en.wikipedia.org/wiki/N-acetylglucosaminehttp://en.wikipedia.org/wiki/Chitinhttp://en.wikipedia.org/wiki/Ribosehttp://en.wikipedia.org/wiki/DNAhttp://en.wikipedia.org/wiki/Deoxyribosehttp://en.wikipedia.org/wiki/Oligosaccharidehttp://en.wikipedia.org/wiki/Polysaccharidehttp://en.wikipedia.org/wiki/Chemical_formulahttp://en.wikipedia.org/wiki/Stoichiometryhttp://en.wikipedia.org/wiki/Fructosehttp://en.wikipedia.org/wiki/Galactosehttp://en.wikipedia.org/wiki/Glucosehttp://en.wikipedia.org/wiki/Monosaccharidehttp://en.wikipedia.org/wiki/Functional_grouphttp://en.wikipedia.org/wiki/Hydroxylhttp://en.wikipedia.org/wiki/Ketonehttp://en.wikipedia.org/wiki/Aldehydehttp://en.wikipedia.org/wiki/Organic_compoundhttp://en.wikipedia.org/wiki/Developmental_biologyhttp://en.wikipedia.org/wiki/Blood_clottinghttp://en.wikipedia.org/wiki/Pathogenesishttp://en.wikipedia.org/wiki/Fertilizationhttp://en.wikipedia.org/wiki/Immune_systemhttp://en.wikipedia.org/wiki/Chitinhttp://en.wikipedia.org/wiki/Cellulosehttp://en.wikipedia.org/wiki/Glycogenhttp://en.wikipedia.org/wiki/Starchhttp://en.wikipedia.org/wiki/Energyhttp://en.wikipedia.org/wiki/Biomoleculehttp://en.wikipedia.org/wiki/Sugarhttp://en.wikipedia.org/wiki/Greek_languagehttp://en.wikipedia.org/wiki/Carbonhttp://en.wikipedia.org/wiki/Hydrate -
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*lipid = organic compound form of carbon, hydrogen, and oxygen examples are fats and cholesterol.
Proteins are large organic compounds made ofamino acids arranged in a linear chain and joined together bypeptidebonds between the carboxyl and amino groups of adjacent amino acid residues. The sequence of amino acids in a
protein is defined by agene and encoded in the genetic code. Although this genetic code specifies 20 "standard" amino
acids plus selenocysteine and - in certain archaea- pyrrolysine, the residues in a protein are sometimes chemically
altered in post-translational modification. This can happen either before the protein is used in the cell, or as part ofcontrol mechanisms. Proteins can also work together to achieve a particular function, and they often associate to form
stable complexes.
Like other biological macromolecules such as polysaccharides and nucleic acids, proteins are essential parts of
organisms and participate in every process within cells. Many proteins are enzymes thatcatalyze biochemical reactions
and are vital to metabolism. Proteins also have structural or mechanical functions, such as actin and myosin in muscle
and the proteins in the cytoskeleton, which form a system ofscaffoldingthat maintains cell shape. Other proteins are
important in cell signaling, immune responses, cell adhesion, and the cell cycle. Proteins are also necessary in animals'
diets, since animals cannot synthesize all the amino acids they need and must obtain essential amino acids from food.
Through the process ofdigestion, animals break down ingested protein into free amino acids that are then used in
metabolism.
The wordproteincomes from the Greekword (proteios) "primary". Proteins were first described and namedby the Swedish chemistJns Jakob Berzelius in 1838. However, the central role of proteins in living organisms was not
fully appreciated until 1926, when James B. Sumner showed that the enzyme ureasewas a protein.The first protein to
be sequenced was insulin, byFrederick Sanger, who won the Nobel Prize for this achievement in 1958. The first
protein structures to be solved included hemoglobin and myoglobin, byMax Perutz and Sir John Cowdery Kendrew,
respectively, in 1958.The three-dimensional structures of both proteins were first determined by x-ray diffraction
analysis; Perutz and Kendrew shared the 1962 Nobel Prize in Chemistryfor these discoveries.
*proten = a complex nitrogenous substance; the main building materials of cells.
2. Monosaccharides, disaccharides, and polysaccharides are carbohydrates; distinguish each of them and give example.
Answer;
Monosaccharides are the simplest carbohydrates in that they cannot be hydrolyzed to smaller carbohydrates.
Monosaccharides are classified according to three different characteristics: the placement of its carbonyl group, the
number ofcarbon atoms it contains, and its chiral handedness. If the carbonyl group is an aldehyde, the
monosaccharide is an aldose; if the carbonyl group is aketone, the monosaccharide is aketose. Monosaccharides with
three carbon atoms are called trioses, those with four are called tetroses, five are called pentoses, six are hexoses, and
so on. These two systems of classification are often combined. For example, glucose is an aldohexose (a six-carbon
aldehyde), ribose is an aldopentose (a five-carbon aldehyde), and fructose is aketohexose (a six-carbon ketone).
Each carbon atom bearing ahydroxyl group (-OH), with the exception of the first and last carbons, are asymmetric,
making them stereocenterswith two possible configurations each (R or S). Because of this asymmetry, a number of
isomers may exist for any given monosaccharide formula. The aldohexose D-glucose, for example, has the formula
(CH2O)6, of which all but two of its six carbons atoms are stereogenic, making D-glucose one of 24
= 16 possible
stereoisomers. In the case ofglyceraldehyde, an aldotriose, there is one pair of possible stereoisomers, which areenantiomers and epimers. 1,3-dihydroxyacetone, the ketose corresponding to the aldose glyceraldehyde, is a
symmetric molecule with no stereocenters). The assignment of D or L is made according to the orientation of the
asymmetric carbon furthest from the carbonyl group: in a standard Fischer projection if the hydroxyl group is on the
right the molecule is a D sugar, otherwise it is an L sugar. Because D sugars are biologically far more common, the D
is often omitted.
*Simple sugar that contain 3 to 7 carbon atoms.
http://en.wikipedia.org/wiki/Organic_compoundhttp://en.wikipedia.org/wiki/Amino_acidhttp://en.wikipedia.org/wiki/Peptide_bondhttp://en.wikipedia.org/wiki/Peptide_bondhttp://en.wikipedia.org/wiki/Carboxylhttp://en.wikipedia.org/wiki/Aminohttp://en.wikipedia.org/wiki/Residue_(chemistry)http://en.wikipedia.org/wiki/Genehttp://en.wikipedia.org/wiki/Genetic_codehttp://en.wikipedia.org/wiki/Selenocysteinehttp://en.wikipedia.org/wiki/Archaeahttp://en.wikipedia.org/wiki/Pyrrolysinehttp://en.wikipedia.org/wiki/Post-translational_modificationhttp://en.wikipedia.org/wiki/Cell_(biology)http://en.wikipedia.org/wiki/Protein_complexhttp://en.wikipedia.org/wiki/Macromoleculeshttp://en.wikipedia.org/wiki/Polysaccharidehttp://en.wikipedia.org/wiki/Nucleic_acidhttp://en.wikipedia.org/wiki/Cell_(biology)http://en.wikipedia.org/wiki/Enzymehttp://en.wikipedia.org/wiki/Catalysishttp://en.wikipedia.org/wiki/Metabolismhttp://en.wikipedia.org/wiki/Actinhttp://en.wikipedia.org/wiki/Myosinhttp://en.wikipedia.org/wiki/Cytoskeletonhttp://en.wikipedia.org/wiki/Scaffoldinghttp://en.wikipedia.org/wiki/Cell_signalinghttp://en.wikipedia.org/wiki/Antibodyhttp://en.wikipedia.org/wiki/Cell_adhesionhttp://en.wikipedia.org/wiki/Cell_cyclehttp://en.wikipedia.org/wiki/Essential_amino_acidhttp://en.wikipedia.org/wiki/Digestionhttp://en.wikipedia.org/wiki/Greek_languagehttp://en.wikipedia.org/wiki/J%C3%B6ns_Jakob_Berzeliushttp://en.wikipedia.org/wiki/James_B._Sumnerhttp://en.wikipedia.org/wiki/Ureasehttp://en.wikipedia.org/wiki/Insulinhttp://en.wikipedia.org/wiki/Frederick_Sangerhttp://en.wikipedia.org/wiki/Hemoglobinhttp://en.wikipedia.org/wiki/Myoglobinhttp://en.wikipedia.org/wiki/Max_Perutzhttp://en.wikipedia.org/wiki/John_Kendrewhttp://en.wikipedia.org/wiki/Nobel_Prize_in_Chemistryhttp://en.wikipedia.org/wiki/Carbonylhttp://en.wikipedia.org/wiki/Carbonhttp://en.wikipedia.org/wiki/Chirality_(chemistry)http://en.wikipedia.org/wiki/Aldehydehttp://en.wikipedia.org/wiki/Aldosehttp://en.wikipedia.org/wiki/Ketonehttp://en.wikipedia.org/wiki/Ketosehttp://en.wikipedia.org/wiki/Triosehttp://en.wikipedia.org/wiki/Tetrosehttp://en.wikipedia.org/wiki/Pentosehttp://en.wikipedia.org/wiki/Hexosehttp://en.wikipedia.org/wiki/Glucosehttp://en.wikipedia.org/wiki/Aldohexosehttp://en.wikipedia.org/wiki/Ribosehttp://en.wikipedia.org/wiki/Aldopentosehttp://en.wikipedia.org/wiki/Fructosehttp://en.wikipedia.org/wiki/Ketohexosehttp://en.wikipedia.org/wiki/Hydroxyl_grouphttp://en.wikipedia.org/wiki/Chirality_(chemistry)http://en.wikipedia.org/wiki/Stereogenichttp://en.wikipedia.org/wiki/Isomerhttp://en.wikipedia.org/wiki/Stereoisomerhttp://en.wikipedia.org/wiki/Glyceraldehydehttp://en.wikipedia.org/wiki/Enantiomershttp://en.wikipedia.org/wiki/Epimerhttp://en.wikipedia.org/wiki/Dihydroxyacetonehttp://en.wikipedia.org/wiki/Dihydroxyacetonehttp://en.wikipedia.org/wiki/Epimerhttp://en.wikipedia.org/wiki/Enantiomershttp://en.wikipedia.org/wiki/Glyceraldehydehttp://en.wikipedia.org/wiki/Stereoisomerhttp://en.wikipedia.org/wiki/Isomerhttp://en.wikipedia.org/wiki/Stereogenichttp://en.wikipedia.org/wiki/Chirality_(chemistry)http://en.wikipedia.org/wiki/Hydroxyl_grouphttp://en.wikipedia.org/wiki/Ketohexosehttp://en.wikipedia.org/wiki/Fructosehttp://en.wikipedia.org/wiki/Aldopentosehttp://en.wikipedia.org/wiki/Ribosehttp://en.wikipedia.org/wiki/Aldohexosehttp://en.wikipedia.org/wiki/Glucosehttp://en.wikipedia.org/wiki/Hexosehttp://en.wikipedia.org/wiki/Pentosehttp://en.wikipedia.org/wiki/Tetrosehttp://en.wikipedia.org/wiki/Triosehttp://en.wikipedia.org/wiki/Ketosehttp://en.wikipedia.org/wiki/Ketonehttp://en.wikipedia.org/wiki/Aldosehttp://en.wikipedia.org/wiki/Aldehydehttp://en.wikipedia.org/wiki/Chirality_(chemistry)http://en.wikipedia.org/wiki/Carbonhttp://en.wikipedia.org/wiki/Carbonylhttp://en.wikipedia.org/wiki/Nobel_Prize_in_Chemistryhttp://en.wikipedia.org/wiki/John_Kendrewhttp://en.wikipedia.org/wiki/Max_Perutzhttp://en.wikipedia.org/wiki/Myoglobinhttp://en.wikipedia.org/wiki/Hemoglobinhttp://en.wikipedia.org/wiki/Frederick_Sangerhttp://en.wikipedia.org/wiki/Insulinhttp://en.wikipedia.org/wiki/Ureasehttp://en.wikipedia.org/wiki/James_B._Sumnerhttp://en.wikipedia.org/wiki/J%C3%B6ns_Jakob_Berzeliushttp://en.wikipedia.org/wiki/Greek_languagehttp://en.wikipedia.org/wiki/Digestionhttp://en.wikipedia.org/wiki/Essential_amino_acidhttp://en.wikipedia.org/wiki/Cell_cyclehttp://en.wikipedia.org/wiki/Cell_adhesionhttp://en.wikipedia.org/wiki/Antibodyhttp://en.wikipedia.org/wiki/Cell_signalinghttp://en.wikipedia.org/wiki/Scaffoldinghttp://en.wikipedia.org/wiki/Cytoskeletonhttp://en.wikipedia.org/wiki/Myosinhttp://en.wikipedia.org/wiki/Actinhttp://en.wikipedia.org/wiki/Metabolismhttp://en.wikipedia.org/wiki/Catalysishttp://en.wikipedia.org/wiki/Enzymehttp://en.wikipedia.org/wiki/Cell_(biology)http://en.wikipedia.org/wiki/Nucleic_acidhttp://en.wikipedia.org/wiki/Polysaccharidehttp://en.wikipedia.org/wiki/Macromoleculeshttp://en.wikipedia.org/wiki/Protein_complexhttp://en.wikipedia.org/wiki/Cell_(biology)http://en.wikipedia.org/wiki/Post-translational_modificationhttp://en.wikipedia.org/wiki/Pyrrolysinehttp://en.wikipedia.org/wiki/Archaeahttp://en.wikipedia.org/wiki/Selenocysteinehttp://en.wikipedia.org/wiki/Genetic_codehttp://en.wikipedia.org/wiki/Genehttp://en.wikipedia.org/wiki/Residue_(chemistry)http://en.wikipedia.org/wiki/Aminohttp://en.wikipedia.org/wiki/Carboxylhttp://en.wikipedia.org/wiki/Peptide_bondhttp://en.wikipedia.org/wiki/Peptide_bondhttp://en.wikipedia.org/wiki/Amino_acidhttp://en.wikipedia.org/wiki/Organic_compound 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Example: Glucose (main blood sugar), Fructose (found in fruits), Galactose(milk sugar),
Deoxyribose( DNA), Ribose(RNA)
Disaccharide is asugar (acarbohydrate) composed of two monosaccharides.Example:
Common disaccharides
Disaccharide Unit 1 Unit 2 Bond
Sucrose (table sugar, cane sugar, saccharose, or beet sugar) glucose fructose (12)
Lactose (milk sugar) galactose glucose (14)
Maltose glucose glucose (14)
Trehalose glucose glucose (11)
Cellobiose glucose glucose (14)
Maltose and cellobiose are hydrolysis products of the polysaccharides, starch and cellulose, respectively.
Less common disaccharides include:
Disaccharide Units Bond
Gentiobiose two glucose monomers (16)
Isomaltose two glucose monomers (16)
Kojibiose two glucose monomers (12)[3]
Laminaribiose two glucose monomers (13)
http://en.wikipedia.org/wiki/Sugarhttp://en.wikipedia.org/wiki/Carbohydratehttp://en.wikipedia.org/wiki/Monosaccharidehttp://en.wikipedia.org/wiki/Sucrosehttp://en.wikipedia.org/wiki/Glucosehttp://en.wikipedia.org/wiki/Glucosehttp://en.wikipedia.org/wiki/Fructosehttp://en.wikipedia.org/wiki/Fructosehttp://en.wikipedia.org/wiki/Lactosehttp://en.wikipedia.org/wiki/Galactosehttp://en.wikipedia.org/wiki/Galactosehttp://en.wikipedia.org/wiki/Maltosehttp://en.wikipedia.org/wiki/Maltosehttp://en.wikipedia.org/wiki/Trehalosehttp://en.wikipedia.org/wiki/Trehalosehttp://en.wikipedia.org/wiki/Cellobiosehttp://en.wikipedia.org/wiki/Cellobiosehttp://en.wikipedia.org/wiki/Hydrolysishttp://en.wikipedia.org/wiki/Polysaccharidehttp://en.wikipedia.org/wiki/Starchhttp://en.wikipedia.org/wiki/Cellulosehttp://en.wikipedia.org/wiki/Gentiobiosehttp://en.wikipedia.org/wiki/Gentiobiosehttp://en.wikipedia.org/wiki/Glucosehttp://en.wikipedia.org/wiki/Monomerhttp://en.wikipedia.org/wiki/Isomaltosehttp://en.wikipedia.org/wiki/Isomaltosehttp://en.wikipedia.org/wiki/Glucosehttp://en.wikipedia.org/wiki/Monomerhttp://en.wikipedia.org/wiki/Kojibiosehttp://en.wikipedia.org/wiki/Kojibiosehttp://en.wikipedia.org/wiki/Glucosehttp://en.wikipedia.org/wiki/Monomerhttp://en.wikipedia.org/wiki/Disaccharide#cite_note-2http://en.wikipedia.org/wiki/Disaccharide#cite_note-2http://en.wikipedia.org/wiki/Disaccharide#cite_note-2http://en.wikipedia.org/wiki/Laminaribiosehttp://en.wikipedia.org/wiki/Laminaribiosehttp://en.wikipedia.org/wiki/Glucosehttp://en.wikipedia.org/wiki/Monomershttp://en.wikipedia.org/wiki/Monomershttp://en.wikipedia.org/wiki/Glucosehttp://en.wikipedia.org/wiki/Laminaribiosehttp://en.wikipedia.org/wiki/Disaccharide#cite_note-2http://en.wikipedia.org/wiki/Monomerhttp://en.wikipedia.org/wiki/Glucosehttp://en.wikipedia.org/wiki/Kojibiosehttp://en.wikipedia.org/wiki/Monomerhttp://en.wikipedia.org/wiki/Glucosehttp://en.wikipedia.org/wiki/Isomaltosehttp://en.wikipedia.org/wiki/Monomerhttp://en.wikipedia.org/wiki/Glucosehttp://en.wikipedia.org/wiki/Gentiobiosehttp://en.wikipedia.org/wiki/Cellulosehttp://en.wikipedia.org/wiki/Starchhttp://en.wikipedia.org/wiki/Polysaccharidehttp://en.wikipedia.org/wiki/Hydrolysishttp://en.wikipedia.org/wiki/Cellobiosehttp://en.wikipedia.org/wiki/Trehalosehttp://en.wikipedia.org/wiki/Maltosehttp://en.wikipedia.org/wiki/Galactosehttp://en.wikipedia.org/wiki/Lactosehttp://en.wikipedia.org/wiki/Fructosehttp://en.wikipedia.org/wiki/Glucosehttp://en.wikipedia.org/wiki/Sucrosehttp://en.wikipedia.org/wiki/Monosaccharidehttp://en.wikipedia.org/wiki/Carbohydratehttp://en.wikipedia.org/wiki/Sugar -
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Mannobiose two mannose monomers either (12), (13), (14), or (16)
Melibiose aglucose monomer and agalactose monomer (16)
Nigerose two glucose monomers (13)
Rutinose arhamnose monomer and aglucose monomer (16)
Xylobiose two xylopyranose monomers (14)
Polysaccharides represent an important class of biological polymers. Their function in living organisms is usually eitherstructure or storage related. Starch (a polymer of glucose) is used as a storage polysaccharide in plants, being found in
the form of both amylose and the branched amylopectin. In animals, the structurally similar glucose polymer is the
more densely branched glycogen, sometimes called 'animal starch'. Glycogen's properties allow it to be metabolized
more quickly, which suits the active lives of moving animals.
Cellulose and chitin are examples of structural polysaccharides. Cellulose is used in the cell walls of plants and other
organisms, and is claimed to be the most abundant organic molecule on earth. It has many uses such as a significant
role in the paper and textile industries, and is used as a feedstock for the production of rayon (via the viscose process),
cellulose acetate, celluloid, and nitrocellulose. Chitin's structure has a similar structure, but has nitrogen containing side
branches, increasing its strength. It is found in arthropod exoskeletons and in the cell walls of some fungi. It also has
multiple uses, includingsurgical threads.Other polysaccharides include callose or laminarin, xylan, mannan, fucoidan,
and galactomannan.
3. Define and familiarized yourself with the ff. processes involved in carbohydrate metabolism
A. Glycolysis- breakdown of glucose to pyruvic acid.
B. Krebs Cycle- eroxic pathways with the mitocondria in which energy is liberated during metabolism of
carbohydrates, fats, amino acid, and CO2 is produced.
C. Glycogenesis- syntesis of glycogen, pathway converts glucose into glycogen.
D. Glycogenolysis- pathway breakdown glycogen into glucose.
E. Gluconeogenesis- convertion of non-carbohydrate molecules (amino acid, lactic acid, glycerol) into glucose.
4. What is the importance of glucose in the body? How does the body store and release glucose to and from tissue?
Answer: glucose is important in the body because it is the principal sugar in the blood, a monosaccharide.
Glucose is a simple monosaccharide sugar and is used as a source of energy in animals and plants. Glucose is one ofthe smallest units which have the characteristics of this class of carbohydrates. The body digests carbohydrates in
foods, transforming them into glucose, which serves as the primary fuel for the brain and muscles. Glucose is also
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called blood sugar as it circulates in the blood at a concentration of 65-110 mg/mL of blood. The most common
form of this sugar is called dextroglucose, commonly referred to as dextrose. Glucose is a monosaccharide
containing six carbon atoms. Chemically joined together, glucose and fructose form sucrose. Starch, cellulose, and
glycogen are common glucose polymers (polysaccharides).
Glucose is the end product of carbohydrate metabolism and is the chief source of energy for living organisms. The
human bodyconverts most dietary carbohydrates into a substance called blood sugar or glucose. In respiration ,
through a series of enzyme-catalysed reactions, glucose is oxidized to eventually form carbon dioxide and water,
yielding energy, mostly in the form of ATP. Glucose is one of the main products of photosynthesis and starts
respiration. Blood glucose concentrations are kept within a relatively narrow range by such factors as hepatic and
renal uptake and release, glucose removal by peripheral tissues, hormone influences on uptake and release, and
intestinal absorption. The normal concentration of glucose in the blood is about 0.1%, but it becomes much higher
in persons suffering from diabetes. Insulin is the main hormone that affects glucose blood levels. When glucose
levels fall to hypoglycemic levels, cells cannot function normally, and symptoms develop such as nervousness, cool
skin, headache, confusion, convulsions or coma.Glucose is found in the sap of plants, and is found in the human
bloodstream , where it is referred to as "blood sugar". The only endogenous sources of glucose are the liver and
kidneys which convert glucose-6-phosphate to glucose. Glucose is usually manufactured by hydrolysis of cornstarch
with steam and dilute acid. Liquid glucose is known as corn syrup in the USA. The corn syrup thus obtained
contains also some dextrins and maltose. When glucose is mixed with maple syrup, it is called pancake syrup.
Industrially glucose is used in the manufacture of candy, chewing gum, jams, jellies, table syrups, and other foods,
and for many other purposes. Glucose is most commonly used in confectionery to give elasticity to caramel or sugar
piece and to help prevent crystallization. It can also be added to chocolate to produce a modeling paste.
Glucose's role in metabolismCarbohydrates are the human body's key source of energy. Glucose is absorbed into the bloodstream through the
intestinal wall. Only the monosaccharides glucose, fructose and galactose are absorbed in humans. Breakdown of
carbohydrates yields mono- and disaccharides, most of which is glucose. Oxidation of glucose is known as
glycolysis. Glucose is oxidized to either lactate or pyruvate. Two different pathways are involved in the metabolism
of glucose: one anaerobic and one aerobic
. The anaerobic process occurs in the cytoplasm and is only moderately efficient. The aerobic cycle takes place in
the mitochondria and is results in the greatest release of energy. Under aerobic conditions, the dominant product in
most tissues is pyruvate and the pathway is known as aerobic glycolysis. Through glycolysis, glucose is directly
involved in the production of ATP, the cell's energy carrier. The NADH generated during glycolysis is used to fuel
mitochondrial ATP synthesis via oxidative phosphorylation, producing either two or three equivalents of ATP
depending upon whether the glycerol phosphate shuttle or the malate-aspartate shuttle is used to transport the
electrons from cytoplasmic NADH into the mitochondria.
Glucose is a major source of energy for most cells of the body. Some of glucose goes directly to fuel brain cells,
while the rest makes its way to the liver and muscles, where it is stored as glycogen, and to fat cells, where it is stored
as fat. Glycogen is the body's auxiliary energy source, tapped and converted back into glucose when it needs more
energy. Although stored fat can also serve as a backup source of energy, it is never directly converted into glucose.
The fructose and galactose are taken up by the liver, where they are converted into glucose. Glucose in the
bloodstream diffuses into the cytoplasm and is locked there by phosphorylation. A glucose molecule is then
rearranged slightly to fructose and phosphorylated again to fructose diphosphate. Glucose is vital to brain function.
The brain requires that glucose concentrations in the blood remain within a certain range in order to function
normally. Glucose metabolism is disturbed in depression, manic-depression, anorexia, and bulimia. In addition,
Alzheimers patients, for instance, register much lower glucose levels than those with other forms of brain
malfunction that resulted from stroke or other vascular disease.
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5. Describe the different lipids in the body
a. Fats - consist of a wide group of compounds that are generally soluble in organic solvents and largely insoluble inwater. Chemically, fats are generallytriesters ofglycerol and fatty acids. Fats may be either solid or liquid at normal
room temperature, depending on their structure and composition. Although the words "oils", "fats", and "lipids" are all
used to refer to fats, "oils" is usually used to refer to fats that are liquids at normal room temperature, while "fats" is
usually used to refer to fats that are solids at normal room temperature. "Lipids" is used to refer to both liquid and solidfats, along with other related substances. The word "oil" is used for any substance that does not mix with water and has
a greasy feel, such as petroleum (or crude oil) and heating oil, regardless of its chemical structure.[1]
Fats form a category oflipid, distinguished from other lipids by their chemical structure and physical properties. This
category of molecules is important for many forms of life, serving both structural and metabolic functions. They are an
important part of the dietof mostheterotrophs (including humans). Fats or lipids are broken down in the body by
enzymes called lipases produced in the pancreas.
Examples of edible animal fats are lard (pig fat), fish oil, and butter or ghee. They are obtained from fats in the milk,
meat and under the skin of the animal. Examples of edible plant fats are peanut, soya bean, sunflower, sesame,
coconut, olive, and vegetable oils. Margarine and vegetable shortening, which can be derived from the above oils, are
used mainly for baking.
B. Phospholipids major lipid component of cell membrane.
C. Steroids are basically flat molecules form of four interlocking rings, thus their structure differs quite a bit from that
of fats.like fats it is made largely of hydrogen and carbon atoms and are fat soluble.
D.Prostaglandins - prostaglandin is any member of a group oflipid compounds that are derived enzymatically fromfatty acids and have important functions in the animal body. Every prostaglandin contains 20 carbon atoms, including a
5-carbon ring. They are mediators and have a variety of strongphysiological effects; although they are technically
hormones, they are rarely classified as such.
The prostaglandins together with the thromboxanes and prostacyclins form the prostanoid class of fatty acid
derivatives; the prostanoid class is a subclass ofeicosanoids.
6. What is the difference between the saturated and unsaturated fatty acid; what is their clinical significance?
Answer: A saturated fattyacid is one in which all the carbons along the chain have two hydrogen
molecules bonded to them, with the exception of the last carbon which has three hydrogen molecules attached (this is
called the omega carbon), have no double bonds and are very rigid and hard, found in high amounts in things like
butter, coconut oil, palm kernel oil and beef fat.
Unsaturated fattyacid the formation of a double bond between two carbon molecules.
Omega-6 vs. Omega-3Over the past 100 years a dramatic change in our diet has occurred. We have invented an industry of prepared foods
made in factories and shipped to consumers viasupermarkets. With this invention, shelf-life became apremium. EFAs, on the other hand, kill shelf-life because they have a tendency to go rancid when exposed to heat,
light and oxygen. At the same time, large commercial oil manufacturers began producing the refined vegetable oils we
are now so familiar with. Currently, 4 oils (soybean, cottonseed, corn, and canola) account for 96% of the vegetable oil
use in the U.S. The w6:w3 ratio of these combined oils is between 12:1 and 25:1. An estimate of the w6:w3 ratio in our
diet 100 years ago is between 3:1 and 5:1. This dramatic shift toward w6 oil consumption, coupled with the alteration
of the fats via hydrogenation and oxidation is thought to be one of the leading factors in the rise of chronic illnesses,
especially cardiovascular diseases over the past century. Modern agricultural practices have a dramatic effect on the
EFA ratios of animal products. For example, a free-range chicken egg has a w6:w3 ratio of 1.3, while a corn fed USDA
chicken egg has a w6:w3 of 19.4 (1). To regain a balanced w6:w3 ratio in our diet is almost impossible without
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supplementing our diets with high levels of w-3 containing oils such as flaxseed oil or concentrated fish oil
supplements. Recommended levels of linoleic acid (omega-6 EFA) are 6-9 grams per day (3-5% of total calories)
and alpha-linolenic acid (omega-3 EFA) are 4-6 grams per day (2-3% of total calories). Of course, therapeutic levels
may exceed these several-fold with almost no toxicity known for these substances.
Therapeutic use of Omega-3fatty acidsTherapeutic uses of the omega-3 essential fatty acid linolenic acid, and its derivatives EPA and DHA (usually from
fish oil) have become more prevalent in the past several decades. Omega 3 fatty acids have been used therapeutically
for cardiovascular diseases, hypertension, inflammatory and autoimmune disorders, cancer, diabetes and several lipid
disorder/deficiency syndromes.Omega 3 and Cardiovascular EffectsRecent interest in omega-3 fatty acids stems from the fatty acid profile and low rate of coronary heart disease
discovered among Greenland Eskimos. While having a diet high in total fat, they consumed a high proportion of
marine fats (seal, whale, and fish). These fats contain high amounts of the long chain, highly-unsaturated, omega-3 fatty
acids (EPA and DHA), originally made by plankton and consumed by these marine animals. A current review has
concluded that omega-3 fatty acids prevent heart disease through the following actions:
Prevention of arrhythmias (ventricular tachycardia
and fibrillation)
formation of and competition against various
prostaglandins and leukotrienes
anti-inflammatory properties (partly byprostaglandin effect)
antithrombotic effect
hypolipidemic effect on triglycerides and VLDLs
inhibition of atherosclerosis.
We will briefly summarize some of the more important aspects of these activities. Induced cardiac arrhthymias, in
both animal and cell culture studies, were halted by the administration of EPA and DHA. The mechanism seems to
be related to the PUFAs ability to stabilize the membrane excitability of heart cells that leads to arrhthymia. While
these experiments cannot be reproduced in humans (ethically), a population case- controlled study showed that
increased intake of long-chain omega-3 fatty acids from seafood is associated with a reduced risk of primary cardiac
arrests .Additionally, patients advised to eat fatty fish after recovering from a myocardial infarction had a 29%
reduction in mortality in the following 2 years than those not advised to do so. A similar secondary prevention trial was
also done using increased levels of the essential fatty acid linolenic acid (18:3w3) (7). 302 patients were randomly
selected and placed on an LNA-rich diet after a first myocardial infarction, another 303 patients were placed on anormal post-infarct prudent diet. After two years, the group receiving the LNA- rich diet had 70% fewer fatal and non-
fatal myocardial infarctions as well as a 70% reduction in overall mortality. The use of flaxseed oil and fish oil should
be considered to reduce the risk of primary cardiac arrest and certainly as a post infarct secondary prevention. A
recent review discusses the aspects of using long-chain omega-3 fatty acids from fish oil as prevention for therosclerosis.
The mechanism of action includes modification of lipid profile (lower triglycerides, lower cholesterol concentration,
increased HDL), moderate reduction in blood pressure, a shift in eicosanoid patterns (increased vasodilation,
decreased platelet aggregation) and a decrease in platelet-derived growth factor (thought to play a role in
atherosclerosis). The data, while promising in the prevention of atherosclerosis, is less conclusive for reversing
already formed plaques.
Perhaps the most conclusive therapeutic result using fish oils is the reduction of serum triglycerides. Studies have
shown that the consumption of fish oil reduces cholesterol levels moderately and tryglycerides significantly.
7. Where would you classify cholesterol?
Answer: Cholesterol is classified as a lipid, the most abundant steroid in animal t issues located in cell membranes and
use for synthesis of steroid hormones and biles salts.
8. Enumerate some example of steroids, which are hormones?
Answer: Steroid hormones
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Sex steroids are a subset ofsex hormones that produce sex differences or supportreproduction. They include
androgens, estrogens, and progestagens.
Corticosteroids include glucocorticoids and mineralocorticoids. Glucocorticoids regulate many aspects ofmetabolism
and immune function, whereas mineralocorticoids help maintain blood volume and control renal excretion of
electrolytes.
Anabolic steroids are a class of steroids that interact with androgen receptors to increase muscle and bone synthesis.
There are natural and synthetic anabolic steroids. In popular language the word "steroids" usually refers to anabolic
steroids.
Cholesterolwhich modulates the fluidity ofcell membranes and is the principle constituent of the plaques implicated
in atherosclerosis.
9. Amino acids are the building blocks of proteins, familiarize yourself with them.
Amino Acid Abbrev. Remarks
Alanine A Ala Very abundant, very versatile. More stiff than glycine, but small enough to pose only smallsteric limits for the protein conformation. It behaves fairly neutrally, can be located in bothhydrophilic regions on the protein outside and the hydrophobic areas inside.
Cysteine C Cys
The sulfur atom binds readily to heavy metal ions. Under oxidizing conditions, two cysteines
can join together in adisulfide bond to form the amino acid cystine. When cystines are part of
a protein, insulin for example, this stabilises tertiary structure and makes the protein more
resistant to denaturation; disulfide bridges are therefore common in proteins that have to
function in harsh environments including digestive enzymes (e.g., pepsin and chymotrypsin)
and structural proteins (e.g., keratin). Disulfides are also found in peptides too small to hold a
stable shape on their own (eg. insulin).
Aspartic acid D AspBehaves similarly to glutamic acid. Carries a hydrophilic acidic group with strong negative
charge. Usually is located on the outer surface of the protein, making it water-soluble. Binds
to positively-charged molecules and ions, often used in enzymes to fix the metal ion. When
located inside of the protein, aspartate and glutamate are usually paired with arginine and
lysine.
Glutamic acid E Glu Behaves similar to aspartic acid. Has longer, slightly more flexible side chain.
Phenylalanine F PheEssential for humans. Phenylalanine, tyrosine, and tryptophan contain large rigid aromatic
group on the side chain. These are the biggest amino acids. Like isoleucine, leucine and
valine, these are hydrophobic and tend to orient towards the interior of the folded protein
molecule.
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Glycine G GlyBecause of the two hydrogen atoms at the carbon, glycine is notoptically active. It is the
smallest amino acid, rotates easily, adds flexibility to the protein chain. It is able to fit into the
tightest spaces, e.g., the triple helix ofcollagen. As too much flexibility is usually not desired,
as a structural component it is less common than alanine.
Histidine H HisIn even slightly acidic conditions protonation of the nitrogen occurs, changing the properties
of histidine and the polypeptide as a whole. It is used by many proteins as a regulatory
mechanism, changing the conformation and behavior of the polypeptide in acidic regions
such as the late endosome or lysosome, enforcing conformation change in enzymes. However
only a few histidines are needed for this, so it is comparatively scarce.
Isoleucine I IleEssential for humans. Isoleucine, leucine and valine have large aliphatic hydrophobic side
chains. Their molecules are rigid, and their mutual hydrophobic interactions are important
for the correct folding of proteins, as these chains tend to be located inside of the protein
molecule.
Lysine K Lys
Essential for humans. Behaves similarly to arginine. Contains a long flexible side-chain with a
positively-charged end. The flexibility of the chain makes lysine and arginine suitable for
binding to molecules with many negative charges on their surfaces. E.g., DNA-binding
proteins have their active regions rich with arginine and lysine. The strong charge makes these
two amino acids prone to be located on the outer hydrophilic surfaces of the proteins; when
they are found inside, they are usually paired with a corresponding negatively-charged amino
acid, e.g., aspartate or glutamate.
Leucine L Leu Essential for humans. Behaves similar to isoleucine and valine. See isoleucine.
Methionine M MetEssential for humans. Always the first amino acid to be incorporated into a protein;
sometimes removed after translation. Like cysteine, contains sulfur, but with a methyl group
instead of hydrogen. This methyl group can be activated, and is used in many reactions where
a new carbon atom is being added to another molecule.
Asparagine N Asn Similar to aspartic acid. Asn contains an amide group where Asp has acarboxyl.
Proline P ProContains an unusual ring to the N-end amine group, which forces the CO-NH amide
sequence into a fixed conformation. Can disrupt protein folding structures like helix orsheet, forcing the desired kink in the protein chain. Common in collagen, where it often
undergoes aposttranslational modification to hydroxyproline. Uncommon elsewhere.
Glutamine Q Gln Similar to glutamic acid. Gln contains an amide group where Glu has acarboxyl. Used inproteins and as a storage for ammonia.
http://en.wikipedia.org/wiki/Glycinehttp://en.wikipedia.org/wiki/Optical_isomerismhttp://en.wikipedia.org/wiki/Collagenhttp://en.wikipedia.org/wiki/Histidinehttp://en.wikipedia.org/wiki/Protonationhttp://en.wikipedia.org/wiki/Endosomehttp://en.wikipedia.org/wiki/Lysosomehttp://en.wikipedia.org/wiki/Isoleucinehttp://en.wikipedia.org/wiki/Essential_amino_acidhttp://en.wikipedia.org/wiki/Lysinehttp://en.wikipedia.org/wiki/Essential_amino_acidhttp://en.wikipedia.org/wiki/Deoxyribonucleic_acidhttp://en.wikipedia.org/wiki/Leucinehttp://en.wikipedia.org/wiki/Essential_amino_acidhttp://en.wikipedia.org/wiki/Methioninehttp://en.wikipedia.org/wiki/Essential_amino_acidhttp://en.wikipedia.org/wiki/Methylhttp://en.wikipedia.org/wiki/Asparaginehttp://en.wikipedia.org/wiki/Asparaginehttp://en.wikipedia.org/wiki/Amidehttp://en.wikipedia.org/wiki/Carboxylhttp://en.wikipedia.org/wiki/Prolinehttp://en.wikipedia.org/wiki/Alpha_helixhttp://en.wikipedia.org/wiki/Alpha_helixhttp://en.wikipedia.org/wiki/Alpha_helixhttp://en.wikipedia.org/wiki/Beta_sheethttp://en.wikipedia.org/wiki/Beta_sheethttp://en.wikipedia.org/wiki/Beta_sheethttp://en.wikipedia.org/wiki/Beta_sheethttp://en.wikipedia.org/wiki/Collagenhttp://en.wikipedia.org/wiki/Posttranslational_modificationhttp://en.wikipedia.org/wiki/Hydroxyprolinehttp://en.wikipedia.org/wiki/Glutaminehttp://en.wikipedia.org/wiki/Glutaminehttp://en.wikipedia.org/wiki/Amidehttp://en.wikipedia.org/wiki/Carboxylhttp://en.wikipedia.org/wiki/Ammoniahttp://en.wikipedia.org/wiki/Ammoniahttp://en.wikipedia.org/wiki/Carboxylhttp://en.wikipedia.org/wiki/Amidehttp://en.wikipedia.org/wiki/Glutaminehttp://en.wikipedia.org/wiki/Hydroxyprolinehttp://en.wikipedia.org/wiki/Posttranslational_modificationhttp://en.wikipedia.org/wiki/Collagenhttp://en.wikipedia.org/wiki/Beta_sheethttp://en.wikipedia.org/wiki/Beta_sheethttp://en.wikipedia.org/wiki/Alpha_helixhttp://en.wikipedia.org/wiki/Prolinehttp://en.wikipedia.org/wiki/Carboxylhttp://en.wikipedia.org/wiki/Amidehttp://en.wikipedia.org/wiki/Asparaginehttp://en.wikipedia.org/wiki/Methylhttp://en.wikipedia.org/wiki/Essential_amino_acidhttp://en.wikipedia.org/wiki/Methioninehttp://en.wikipedia.org/wiki/Essential_amino_acidhttp://en.wikipedia.org/wiki/Leucinehttp://en.wikipedia.org/wiki/Deoxyribonucleic_acidhttp://en.wikipedia.org/wiki/Essential_amino_acidhttp://en.wikipedia.org/wiki/Lysinehttp://en.wikipedia.org/wiki/Essential_amino_acidhttp://en.wikipedia.org/wiki/Isoleucinehttp://en.wikipedia.org/wiki/Lysosomehttp://en.wikipedia.org/wiki/Endosomehttp://en.wikipedia.org/wiki/Protonationhttp://en.wikipedia.org/wiki/Histidinehttp://en.wikipedia.org/wiki/Collagenhttp://en.wikipedia.org/wiki/Optical_isomerismhttp://en.wikipedia.org/wiki/Glycine -
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Arginine R Arg Functionally similar to lysine.
Serine S Ser Serine and threonine have a short group ended with ahydroxyl group. Its hydrogen is easy toremove, so serine and threonine often act as hydrogen donors in enzymes. Both are veryhydrophilic, therefore the outer regions of soluble proteins tend to be rich with them.
Threonine T Thr Essential for humans. Behaves similarly to serine.
Valine V Val Essential for humans. Behaves similarly to isoleucine and leucine. See isoleucine.
Tryptophan W Trp Essential for humans. Behaves similarly to phenylalanine and tyrosine (see phenylalanine).Precursor ofserotonin. Naturaly fluorescent.
Tyrosine Y Tyr Behaves similarly to phenylalanine and tryptophan (see phenylalanine). Precursor ofmelanin,epinephrine, and thyroid hormones. Naturaly fluorescent, although fluorescence is usuallyquenched by energy transfer to tryptophans.
10. Enumerate the important function of proteins in the body.
Functional Group Roles in the body
http://en.wikipedia.org/wiki/Argininehttp://en.wikipedia.org/wiki/Serinehttp://en.wikipedia.org/wiki/Hydroxylhttp://en.wikipedia.org/wiki/Threoninehttp://en.wikipedia.org/wiki/Essential_amino_acidhttp://en.wikipedia.org/wiki/Valinehttp://en.wikipedia.org/wiki/Essential_amino_acidhttp://en.wikipedia.org/wiki/Tryptophanhttp://en.wikipedia.org/wiki/Tryptophanhttp://en.wikipedia.org/wiki/Essential_amino_acidhttp://en.wikipedia.org/wiki/Serotoninhttp://en.wikipedia.org/wiki/Tyrosinehttp://en.wikipedia.org/wiki/Melaninhttp://en.wikipedia.org/wiki/Epinephrinehttp://en.wikipedia.org/wiki/Thyroid_hormonehttp://en.wikipedia.org/wiki/Thyroid_hormonehttp://en.wikipedia.org/wiki/Epinephrinehttp://en.wikipedia.org/wiki/Melaninhttp://en.wikipedia.org/wiki/Tyrosinehttp://en.wikipedia.org/wiki/Serotoninhttp://en.wikipedia.org/wiki/Essential_amino_acidhttp://en.wikipedia.org/wiki/Tryptophanhttp://en.wikipedia.org/wiki/Essential_amino_acidhttp://en.wikipedia.org/wiki/Valinehttp://en.wikipedia.org/wiki/Essential_amino_acidhttp://en.wikipedia.org/wiki/Threoninehttp://en.wikipedia.org/wiki/Hydroxylhttp://en.wikipedia.org/wiki/Serinehttp://en.wikipedia.org/wiki/Arginine -
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Antibodies highly specialize proteins that recognize, bind with, and inactivate (immunoglobulins ) bacteria,toxins,and some viruses, function in the imumune responsewhich helps protect the body from invading foreign substances.Hormones Help to regulate growth and developmnet. Examples include
*growth hormones- an anabolic hormonenecessary for optimal growth.*Insulin- helps regualate blood sugar levels*Nerve growth factor- guides the growth of nuerons in the development ofthe nervous system.
Transport proteins hemogloben transport oxygen in the blood; other transport organism in theblood carry iron, cholesterol, or other substance.
Catalysts (enzymes) essential to virtually every biochemical reaction in the body, increase therates of chemical reactions by at lest a million fold, in their absence(or destruction ) biochamecal reaction cease.
11. What are a dipeptide, tripeptide, and polypeptide; define a peptide bond.
Answer: Dipeptide is a molecule consisting of two amino acidsjoined by a single peptide bondtripeptide is apeptide consisting of three amino acidsjoined bypeptide bonds.Examples of tripeptides are:
Glutathione(-glutamyl-cysteinyl-glycine) is an antioxidant, protecting cells from toxins such as free radicals. Thyrotropin-releasing hormone(TRH, thyroliberin or protirelin) (L-pyroglutamyl-L-histidinyl-L-prolinamide)
is apeptide hormone that stimulates the release ofthyroid-stimulating hormone and prolactin by the anterior
pituitary.
Melanostatin (prolyl-leucyl-glycinamide) is a peptide hormone produced in the hypothalamus that inhibits therelease ofmelanocyte-stimulating hormone (MSH).
Ophthalmic acid(L--glutamyl-L--aminobutyryl-glycine) is an analogue ofglutathione isolated fromcrystalline lens.
Norophthalmic acid (y-glutamyl-alanyl-glycine) is an analogue of glutathione (L-cysteine replaced by L-alanine) isolated from crystalline lens.
Eisenin (pGlu-Gln-Ala-OH) is a peptide with immunological activity isolated from the Japanese marine algaEisenia bicyclis.
Proteins are polypeptide molecules (or consist of multiple polypeptide subunits). The distinction is that peptides areshort and polypeptides/proteins are long. There are several different conventions to determine these, all of which have
caveats and nuances.
http://en.wikipedia.org/wiki/Amino_acidshttp://en.wikipedia.org/wiki/Peptide_bondhttp://en.wikipedia.org/wiki/Peptidehttp://en.wikipedia.org/wiki/Amino_acidshttp://en.wikipedia.org/wiki/Peptide_bondhttp://en.wikipedia.org/wiki/Glutathionehttp://en.wikipedia.org/wiki/Glutathionehttp://en.wikipedia.org/wiki/Antioxidanthttp://en.wikipedia.org/wiki/Free_radicalhttp://en.wikipedia.org/wiki/Thyrotropin-releasing_hormonehttp://en.wikipedia.org/wiki/Thyrotropin-releasing_hormonehttp://en.wikipedia.org/wiki/Peptide_hormonehttp://en.wikipedia.org/wiki/Thyroid-stimulating_hormonehttp://en.wikipedia.org/wiki/Prolactinhttp://en.wikipedia.org/wiki/Anterior_pituitaryhttp://en.wikipedia.org/wiki/Anterior_pituitaryhttp://en.wikipedia.org/wiki/Hypothalamushttp://en.wikipedia.org/wiki/Melanocyte-stimulating_hormonehttp://en.wikipedia.org/wiki/Ophthalmic_acidhttp://en.wikipedia.org/wiki/Ophthalmic_acidhttp://en.wikipedia.org/wiki/Glutathionehttp://en.wikipedia.org/wiki/Lens_(anatomy)http://en.wikipedia.org/wiki/Crystalline_lenshttp://en.wikipedia.org/wiki/Proteinhttp://en.wikipedia.org/wiki/Moleculehttp://en.wikipedia.org/wiki/Moleculehttp://en.wikipedia.org/wiki/Proteinhttp://en.wikipedia.org/wiki/Crystalline_lenshttp://en.wikipedia.org/wiki/Lens_(anatomy)http://en.wikipedia.org/wiki/Glutathionehttp://en.wikipedia.org/wiki/Ophthalmic_acidhttp://en.wikipedia.org/wiki/Melanocyte-stimulating_hormonehttp://en.wikipedia.org/wiki/Hypothalamushttp://en.wikipedia.org/wiki/Anterior_pituitaryhttp://en.wikipedia.org/wiki/Anterior_pituitaryhttp://en.wikipedia.org/wiki/Prolactinhttp://en.wikipedia.org/wiki/Thyroid-stimulating_hormonehttp://en.wikipedia.org/wiki/Peptide_hormonehttp://en.wikipedia.org/wiki/Thyrotropin-releasing_hormonehttp://en.wikipedia.org/wiki/Free_radicalhttp://en.wikipedia.org/wiki/Antioxidanthttp://en.wikipedia.org/wiki/Glutathionehttp://en.wikipedia.org/wiki/Peptide_bondhttp://en.wikipedia.org/wiki/Amino_acidshttp://en.wikipedia.org/wiki/Peptidehttp://en.wikipedia.org/wiki/Peptide_bondhttp://en.wikipedia.org/wiki/Amino_acids -
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Apeptide bond is achemical bond formed between two moleculeswhen the carboxyl group of one molecule reactswith the amino group of the other molecule, thereby releasing a molecule ofwater (H2O). This is adehydration
synthesis reaction (also known as acondensation reaction), and usually occurs between amino acids. The resulting CO-
NH bond is called apeptide bond, and the resulting molecule is an amide. The four-atom functional group -C(=O)NH- is called an amide group or (in the context of proteins) apeptide group. Polypeptides and proteins arechains ofamino acids held together by peptide bonds, as is the backbone ofPNA. Polyamides, such as nylons and
aramids, are synthetic molecules (polymers) that possess peptide bonds.
A peptide bond can be broken byamide hydrolysis (the adding of water). The peptide bonds in proteins are
metastable, meaning that in the presence of water they will break spontaneously, releasing about 10 kJ/mol offree
energy, but this process is extremely slow. In living organisms, the process is facilitated by enzymes. Living organisms
also employ enzymes to form peptide bonds; this process requires free energy. The wavelength ofabsorbance for a
peptide bond is 190-230nm.
12. What are the different levels of proteinstructure, primary, secondary, tertiary, and quaternary
Answer: Most proteins fold into unique 3-dimensional structures. The shape into which a protein naturally folds is
known as its native state. Although many proteins can fold unassisted, simply through the chemical properties of theiramino acids, others require the aid of molecular chaperones to fold into their native states. Biochemists often refer to
four distinct aspects of a protein's structure:
Primary structure: the amino acid sequence Secondary structure: regularly repeating local structures stabilized byhydrogen bonds. The most common
examples are the alpha helix and beta sheet.[12]
Because secondary structures are local, many regions of
different secondary structure can be present in the same protein molecule.
Tertiary structure: the overall shape of a single protein molecule; the spatial relationship of the secondarystructures to one another. Tertiary structure is generally stabilized by nonlocal interactions, most commonly
the formation of ahydrophobic core, but also through salt bridges, hydrogen bonds, disulfide bonds, and
even post-translational modifications. The term "tertiary structure" is often used as synonymous with the term
fold.
Quaternary structure: the shape or structure that results from the interaction of more than one proteinmolecule, usually calledprotein subunitsin this context, which function as part of the larger assembly or
protein complex.
13. What are the enzymes and what are there role in the human body?
Answer: Enzymes are biomolecules thatcatalyze (i.e. increase the rates of) chemical reactions. Almost all enzymes areproteins. In enzymatic reactions, the molecules at the beginning of the process are called substrates, and the enzyme
converts them into different molecules, the products. Almost all processes in a biological cell need enzymes to occur at
significant rates. Since enzymes are selective for their substrates and speed up only a few reactions from among many
possibilities, the set of enzymes made in a cell determines which metabolic pathways occur in that cell.
Like all catalysts, enzymes work by lowering the activation energy(Ea or G
) for a reaction, thus dramatically
increasing the rate of the reaction. Most enzyme reaction rates are millions of times faster than those of comparable
un-catalyzed reactions. As with all catalysts, enzymes are not consumed by the reactions they catalyze, nor do they alter
the equilibrium of these reactions. However, enzymes do differ from most other catalysts by being much more
specific. Enzymes are known to catalyze about 4,000 biochemical reactions. A few RNAmolecules called ribozymes
catalyze reactions, with an important example being some parts of the ribosome. Synthetic molecules called artificial
enzymes also display enzyme-like catalysis.
14. What are the factors that could affect their activity?
http://en.wikipedia.org/wiki/Chemical_bondhttp://en.wikipedia.org/wiki/Moleculehttp://en.wikipedia.org/wiki/Carboxyl_grouphttp://en.wikipedia.org/wiki/Aminehttp://en.wikipedia.org/wiki/Waterhttp://en.wikipedia.org/wiki/Dehydration_synthesishttp://en.wikipedia.org/wiki/Dehydration_synthesishttp://en.wikipedia.org/wiki/Condensation_reactionhttp://en.wikipedia.org/wiki/Amino_acidhttp://en.wikipedia.org/wiki/Amidehttp://en.wikipedia.org/wiki/Polypeptidehttp://en.wikipedia.org/wiki/Proteinhttp://en.wikipedia.org/wiki/Amino_acidhttp://en.wikipedia.org/wiki/Peptide_nucleic_acidhttp://en.wikipedia.org/wiki/Polyamidehttp://en.wikipedia.org/wiki/Nylonhttp://en.wikipedia.org/wiki/Aramidhttp://en.wikipedia.org/wiki/Polymerhttp://en.wikipedia.org/wiki/Amide_hydrolysishttp://en.wikipedia.org/wiki/Metastablehttp://en.wikipedia.org/wiki/Joulehttp://en.wikipedia.org/wiki/Mole_(unit)http://en.wikipedia.org/wiki/Thermodynamic_free_energyhttp://en.wikipedia.org/wiki/Thermodynamic_free_energyhttp://en.wikipedia.org/wiki/Enzymehttp://en.wikipedia.org/wiki/Wavelengthhttp://en.wikipedia.org/wiki/Absorbancehttp://en.wikipedia.org/wiki/Protein_foldinghttp://en.wikipedia.org/wiki/Native_statehttp://en.wikipedia.org/wiki/Chaperone_(protein)http://en.wikipedia.org/wiki/Primary_structurehttp://en.wikipedia.org/wiki/Primary_structurehttp://en.wikipedia.org/wiki/Peptide_sequencehttp://en.wikipedia.org/wiki/Secondary_structurehttp://en.wikipedia.org/wiki/Secondary_structurehttp://en.wikipedia.org/wiki/Hydrogen_bondhttp://en.wikipedia.org/wiki/Alpha_helixhttp://en.wikipedia.org/wiki/Beta_sheethttp://en.wikipedia.org/wiki/Proteins#cite_note-Branden-11http://en.wikipedia.org/wiki/Proteins#cite_note-Branden-11http://en.wikipedia.org/wiki/Proteins#cite_note-Branden-11http://en.wikipedia.org/wiki/Tertiary_structurehttp://en.wikipedia.org/wiki/Tertiary_structurehttp://en.wikipedia.org/wiki/Hydrophobic_corehttp://en.wikipedia.org/wiki/Salt_bridge_(protein)http://en.wikipedia.org/wiki/Disulfide_bondhttp://en.wikipedia.org/wiki/Post-translational_modificationhttp://en.wikipedia.org/wiki/Quaternary_structurehttp://en.wikipedia.org/wiki/Quaternary_structurehttp://en.wikipedia.org/wiki/Protein-protein_interactionhttp://en.wikipedia.org/wiki/Protein_subunithttp://en.wikipedia.org/wiki/Protein_subunithttp://en.wikipedia.org/wiki/Protein_subunithttp://en.wikipedia.org/wiki/Protein_complexhttp://en.wikipedia.org/wiki/Biomoleculehttp://en.wikipedia.org/wiki/Catalysishttp://en.wikipedia.org/wiki/Reaction_ratehttp://en.wikipedia.org/wiki/Chemical_reactionhttp://en.wikipedia.org/wiki/Proteinhttp://en.wikipedia.org/wiki/Moleculehttp://en.wikipedia.org/wiki/Substrate_(biochemistry)http://en.wikipedia.org/wiki/Cell_(biology)http://en.wikipedia.org/wiki/Metabolic_pathwayhttp://en.wikipedia.org/wiki/Activation_energyhttp://en.wikipedia.org/wiki/Chemical_equilibriumhttp://en.wikipedia.org/wiki/RNAhttp://en.wikipedia.org/wiki/Ribozymehttp://en.wikipedia.org/wiki/Ribosomehttp://en.wikipedia.org/wiki/Artificial_enzymehttp://en.wikipedia.org/wiki/Artificial_enzymehttp://en.wikipedia.org/wiki/Artificial_enzymehttp://en.wikipedia.org/wiki/Artificial_enzymehttp://en.wikipedia.org/wiki/Ribosomehttp://en.wikipedia.org/wiki/Ribozymehttp://en.wikipedia.org/wiki/RNAhttp://en.wikipedia.org/wiki/Chemical_equilibriumhttp://en.wikipedia.org/wiki/Activation_energyhttp://en.wikipedia.org/wiki/Metabolic_pathwayhttp://en.wikipedia.org/wiki/Cell_(biology)http://en.wikipedia.org/wiki/Substrate_(biochemistry)http://en.wikipedia.org/wiki/Moleculehttp://en.wikipedia.org/wiki/Proteinhttp://en.wikipedia.org/wiki/Chemical_reactionhttp://en.wikipedia.org/wiki/Reaction_ratehttp://en.wikipedia.org/wiki/Catalysishttp://en.wikipedia.org/wiki/Biomoleculehttp://en.wikipedia.org/wiki/Protein_complexhttp://en.wikipedia.org/wiki/Protein_subunithttp://en.wikipedia.org/wiki/Protein-protein_interactionhttp://en.wikipedia.org/wiki/Quaternary_structurehttp://en.wikipedia.org/wiki/Post-translational_modificationhttp://en.wikipedia.org/wiki/Disulfide_bondhttp://en.wikipedia.org/wiki/Salt_bridge_(protein)http://en.wikipedia.org/wiki/Hydrophobic_corehttp://en.wikipedia.org/wiki/Tertiary_structurehttp://en.wikipedia.org/wiki/Proteins#cite_note-Branden-11http://en.wikipedia.org/wiki/Beta_sheethttp://en.wikipedia.org/wiki/Alpha_helixhttp://en.wikipedia.org/wiki/Hydrogen_bondhttp://en.wikipedia.org/wiki/Secondary_structurehttp://en.wikipedia.org/wiki/Peptide_sequencehttp://en.wikipedia.org/wiki/Primary_structurehttp://en.wikipedia.org/wiki/Chaperone_(protein)http://en.wikipedia.org/wiki/Native_statehttp://en.wikipedia.org/wiki/Protein_foldinghttp://en.wikipedia.org/wiki/Absorbancehttp://en.wikipedia.org/wiki/Wavelengthhttp://en.wikipedia.org/wiki/Enzymehttp://en.wikipedia.org/wiki/Thermodynamic_free_energyhttp://en.wikipedia.org/wiki/Thermodynamic_free_energyhttp://en.wikipedia.org/wiki/Mole_(unit)http://en.wikipedia.org/wiki/Joulehttp://en.wikipedia.org/wiki/Metastablehttp://en.wikipedia.org/wiki/Amide_hydrolysishttp://en.wikipedia.org/wiki/Polymerhttp://en.wikipedia.org/wiki/Aramidhttp://en.wikipedia.org/wiki/Nylonhttp://en.wikipedia.org/wiki/Polyamidehttp://en.wikipedia.org/wiki/Peptide_nucleic_acidhttp://en.wikipedia.org/wiki/Amino_acidhttp://en.wikipedia.org/wiki/Proteinhttp://en.wikipedia.org/wiki/Polypeptidehttp://en.wikipedia.org/wiki/Amidehttp://en.wikipedia.org/wiki/Amino_acidhttp://en.wikipedia.org/wiki/Condensation_reactionhttp://en.wikipedia.org/wiki/Dehydration_synthesishttp://en.wikipedia.org/wiki/Dehydration_synthesishttp://en.wikipedia.org/wiki/Waterhttp://en.wikipedia.org/wiki/Aminehttp://en.wikipedia.org/wiki/Carboxyl_grouphttp://en.wikipedia.org/wiki/Moleculehttp://en.wikipedia.org/wiki/Chemical_bond 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Answer: Enzyme activity can be affected by other molecules. Inhibitors are molecules that decrease enzyme activity;
activators are molecules that increase activity. Manydrugs and poisons are enzyme inhibitors. Activity is also affected
bytemperature, chemical environment (e.g. pH), and the concentration of substrate. Some enzymes are used
commercially, for example, in the synthesis ofantibiotics. In addition, some household products use enzymes to speed
up biochemical reactions (e.g., enzymes in biological washing powders break down protein or fatstains on clothes;
enzymes in meat tenderizers break down proteins, making the meat easier to chew).
15. What are nucleic acids, what are their functions?
Answer: Nucleic acids are organic substances. Nucleic acid molecules are long chains that generally occur in
combination with proteins. The two chief types are DNA (deoxyribonucleic acid), the main constituent of genes, and
RNA (ribonucleic acid), which is involved in protein synthesis and transmission of DNA's genetic information. The
two classes of nucleic acids have backbones that are shaped like helical strands. Their molecular weights are in the
millions. To the backbones are connected a great number of smaller molecules (side groups) of four different types.
Each nucleic acid chain is composed of subunits called nucleotides, each containing a sugar, a phosphate group, and
one of four bases: adenine (symbolized A), guanine (G), cytosine (C), and thymine (T). RNA contains the sugar ribose
instead of the deoxyribose of DNA and the base uracil (U) instead of thymine. The sequence of these molecules on
the strand determines the code of the particular nucleic acid. This code, in turn, signals the cell how to reproduceeither a duplicate of itself or the proteins it requires for survival.
Function
The functions of nucleic acids are the storage, expression and replicationof biological information. DNA carries the
genetic information in its sequence of bases and this must be transmitted from one generation to the next. During
reproduction there must be accurate copying of the base sequence of the DNA so that each of the two new daughter
cells receives a copy of the origional parental genome.
The specific sequences of nucleotides determine the cell's genetic information: each three-nucleotide DNA
sequence specifies one particular amino acid. The long sequences of DNA nucleotides thus correspond to the
sequences of amino acids in the cell's proteins. In order to be expressed as protein, the genetic information is carried
to the protein-synthesizing machinery of the cell, usually in the cell cytoplasm. Forms of RNA mediate this process.
DNA not only provides information but also acts as a blueprint for its own exact replication: The cell replicates its
DNA by making a complementary copy of its exact nucleotide sequence: T for every A, C for every G, G for every C,
A for every T. Although the triplet nucleotide code seems to be universal, the actual sequences of the nucleotides vary
according to the species and individual.
Points to remember:
DNA and RNA are the two main types of nucleic acid DNA is used to pass on heriditary information and RNA is used to aid in the production of proteins the four bases for DNA are adenine, guanine, cytosine, and thymine
16. What are the different nucleic acid , differentiate DNA and RNA?
Answer: genetic information needed for life and the inheritance of characters is encoded in biomolecules known as
nucleic acids. There are two forms of nucleic acid - DNA or deoxyribonucleic acid and RNA or ribonucleic acid, both
of these forms are the basis of all life and occur in all living cells. In chemical structure, these two molecules are linear
and without branching; they are made essentially as polymers of discrete subunits termed the nucleotides - this is the
language in which all life on earth is written, encoded and passed on from one generation to the next. Bacteria- called
http://en.wikipedia.org/wiki/Enzyme_inhibitorhttp://en.wikipedia.org/wiki/Enzyme_activatorhttp://en.wikipedia.org/wiki/Drughttp://en.wikipedia.org/wiki/Poisonhttp://en.wikipedia.org/wiki/Temperaturehttp://en.wikipedia.org/wiki/PHhttp://en.wikipedia.org/wiki/Concentrationhttp://en.wikipedia.org/wiki/Antibiotichttp://en.wikipedia.org/wiki/Washing_powderhttp://en.wikipedia.org/wiki/Fathttp://en.wikipedia.org/wiki/Meat_tenderizerhttp://www.herbs2000.com/h_menu/bacteria.htmhttp://www.herbs2000.com/h_menu/bacteria.htmhttp://en.wikipedia.org/wiki/Meat_tenderizerhttp://en.wikipedia.org/wiki/Fathttp://en.wikipedia.org/wiki/Washing_powderhttp://en.wikipedia.org/wiki/Antibiotichttp://en.wikipedia.org/wiki/Concentrationhttp://en.wikipedia.org/wiki/PHhttp://en.wikipedia.org/wiki/Temperaturehttp://en.wikipedia.org/wiki/Poisonhttp://en.wikipedia.org/wiki/Drughttp://en.wikipedia.org/wiki/Enzyme_activatorhttp://en.wikipedia.org/wiki/Enzyme_inhibitor -
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prokaryotes - along with all the higher organisms collectively called the eukaryotes use DNA as their primary carrier
of genetic information and RNA as an information messenger. This DNA is a part of the nucleus of all eukaryotes as
well as the nucleiod of prokaryotes - prokaryotes include the bacteria, while the eukaryotes form the fungi, higher
plants and animals. While RNA serves as the genetic information carrier in some viruses and is used as the sole
molecule of heredity in these viruses. RNA is used only as a messenger in higher forms of true life excluding the
viruses, in these forms, the RNA molecules are written using the DNA as the template. The RNA encoded
information is than translated into protein, via bio-synthetic mechanism in the cytoplasm of the cell. Thus, DNA
carries all information, which is then transcribed into RNA and then translated into protein - which then performs
necessary vital actions in the living cell. This is called the central dogma of molecular biology.
The basic components of the nucleic acids, the nucleotides are structurally formed from three major units. Every
single nucleotide will consist of one five-carbon pentose sugar - ribose in RNA, and deoxy-ribose in DNA; One flat,
heterocyclic, nitrogen rich organic base and lastly one phosphate group - this last unit of the nucleic acid polymer is
responsible for the acidic nature of the nucleic acid as it is very negative in charge. These components of the nucleic
acids are linked together covalently through a glycosidic bond formed between the sugar unit and the nitrogenous base.
The addition of the phosphate group also covalently connected to the sugar unit completes the basic component of the
nucleic acid polymer.
RNA is made from monomers of the sugar -D-ribose and the sugar along with the nitrogenous base and inorganic
phosphate is called a ribonucleotide -without the phosphate, its a nucleoside. DNA is made of monomers formed by
the pentose sugar deoxy-ribose, along with a nitrogenous base and inorganic phosphate to make a
deoxyribonucleotide. The DNA monomers are differentiated from the RNA monomers by the absence of an oxygen
at the number two carbon in the sugars and are called a 2-deoxy--D-ribose sugars.
The nitrogenous bases can be classed into two basic types of organic bases. Pyrimidines are single-ringed structures
while the purines are double ringed-structures. There are three types of pyrimidines and two types of purines used in
the construction of nucleic acids - all of them are not used in both RNA and DNA, which is the reason for the
difference between the nucleic acids. The bases adenine and guanine are the purines found in both RNA and DNA.
While the pyrimidines come in three types, cytosine, thymine, and uracil - the last replaces thymine in RNA and is not
found in DNA. While the pyrimidine and thymine are found primarily in DNA, uracil is seen only in RNA. A purine
always pair with a pyrimidine and vice versa in a nucleic acid. Along each polynucleotide strand forming DNA or
RNA, all the nucleotides adjacent to each other are joined by covalent bonds called phosphodiester bonds formed
between the number three carbon of one nucleotide and the number five carbon of the nearest nucleotide. In this way
the monomers are interlinked to form a nucleic acid polymer holding all the genetic information necessary for life.
Genetic information is stored along the nucleic acid chain because all the bases in the nucleotides form hydrogen
bonds with each other in a specific way - this ensures what is called base pairing. Base pairing is the key behind the
code formed from four bases. For example, adenine will always combine with thymine in DNA with the formation of
two hydrogen bonds, while guanine will always base pair with cytosine via three hydrogen bonds. Since the hydrogen
formation occurs between two different strands of linear DNA, it results in the formation of a DNA double helix -
formed by two complementary DNA strands holding genetic information. Similarly, adenine can also form hydrogen
bonds with uracil in DNA-RNA hybrid chains as well as in RNA to RNA complexes. In both DNA and RNA, the
base guanine will always form three hydrogen bonds with cytosine. In other words, guanine always pairs with cytosine
in DNA as well as RNA, while adenine pair with thymine in DNA but with uracil in RNA. Viable DNA is found in the
uniform shape of a double helix in chromosomes, each complementary chain is wound around the other complement
in a spiral like a staircase. All nucleic acid chains do not exist in the form of double strands as the RNA molecules that
are synthesized from DNA templates are always in the form of single strands - some viruses which use RNA as agenetic information carrier have double stranded RNA. In the body, a single stranded RNA chain is sometimes folded
back onto itself so as to form complementary base pairs along the length of the chain to produce unique secondary
structures necessary for some biochemical reactions.
Along a DNA double helix, each of the two complementary strands forming the helix are found in opposite directions
to each other, they are said to be anti-parallel in orientation, which means one chain is starts from the 5' phosphate
end, while the other chain starts from the 3' hydroxyl end. In a DNA double helix, the winding of the two chains
results in a turn along the helix at every ten base pairs, this has been measured to be about 3.4 nm - nanometers in
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length. Base pairings occur along the center of the molecule resulting in stacking of the bases along the chain. As the
bases repel water, they form a hydrophobic core at the center and the double helix as a result is approximately two nm
across.
RNA serve as information messengers for the DNA. The code on the DNA chain is copied onto an RNA chain and
this information is translated into a protein, which then affects the desired outcome in the cell. In higher organisms,
RNA comes in three basic types according to the function it performs inside the cell.
The tRNA or transfer RNAs transfer one amino acid at a time during the formation of a protein.
The mRNA or messenger RNAs carry the information written in the DNA to the ribosomes for translation into
protein.
The rRNA or ribosomal RNAs aid in the formation of proteins on ribosomes - which are the protein manufacturing
centers in all cells.
All the different classes of RNA are important for the body. In terms of size, the transfer RNAs or tRNAs are the
smallest of the lot, being approximately about seventy five to eighty nucleotides long - their main action is the
formation of a protein polymer and each tRNA positions single amino acids on the ribosome during the
polymerization reaction to form distinct polypeptide chains - which in turn form proteins. The tRNAs also containadditional and unusual bases along with the normal complement of adenine, guanine, cytosine and uracil in their
chains - this is in keeping with their specialized nature and function. The linear mRNAs differ according to the
information they transcribe from the genetic code in the DNA template. As the genetic code that will specify the
unique amino acid sequence for specific proteins resides in the DNA sequence, it follows that the complementary
ribonucleotide sequences forming the mRNA will be long or short depending on the length and composition of the
template DNA - therefore, mRNA chains are highly variable in length and composition. On the other hand, ribosomal
or rRNAs are integral to the structure of the ribosomes - protein building sites in cells. There are also different types of
rRNAs, there are four main types of rRNAs in eukaryotes while three main classes of rRNAs are found in the
prokaryotes - namely the bacteria and archea.
17. Give the components of nucleotides, what is nitrogenous base, a sugar moiety?
Answer: Nucleotides are the building blocks that form DNA and RNA. A nucleotide consists of three parts: nitrogen
base + 5-carbon sugar + phosphate. If the phosphate is missing and the molecule consists of the nitrogen base and 5-
carbon sugar, it is a nucleoside. The linkage between nitrogen base and 5-carbon sugar is a glycosidic bond.
Nitrogenous bases are organic compounds that owe their basic properties to the lone pair ofelectrons of anitrogenatom. Typical nitrogenous bases are ammonia(NH3), triethylamine, pyridine, and the nucleobases adenine, guanine,
thymine, cytosine, and uracil. Nitrogenous bases can be classified under two groups: purin