Biochemistry
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Transcript of Biochemistry
Biochemistryhttp://www.brainpop.com/science/matterandchemistry/bodychemistry/
Chemistry of Carbon
•Carbon can form covalent bonds with up to 4 other atoms
•Hydrocarbons- compounds made up of only carbon and hydrogen
Giant Molecules from Small Building Blocks
•Macromolecules:
•Structure: Polymers- large molecules made by stringing together many small molecules called monomers
CarbohydratesFats
ProteinsNucleic Acids
4
Basic building blocks
a long train of box cars ?
>3 generally 100-1,000 monomers = Polymer
Polymer
Dimer
MonomerMonomer single building block unit
5
Carbohydrates
C, H, O2:1 ratio of H to OMonosaccharide
–C6H12O6 = glucose, fructose
Disaccharide = 2 mono’s: C12H22O11
–Sucrose, lactose
Polysaccharide = 100’s to 1,000’s–Starch, cellulose, glycogen, chitin
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Cellulose – most common polysaccharide– (estimate - over 1 trillion tons made
by plants/year) Starch (in plants)
– is stored in plant cell vacuoles. Glycogen (in animals) -
– highly branched starch – glycogen. (In mammals, glycogen stored in liver and muscles -
provides a quick source of energy. – Excess glucose ? taken up from the blood - stored where ?
Polysaccharides: are the most abundant organic compounds in the biosphere.
MonomerMonomer
Polymer
Dimer
Dehydration Synthesis: Process in which cells link monomers together to form polymers- Results in loss of water
HH OHOH HH
HH
HH22OO
Hydrolysis: Digestion of macromolecules through the addition of water
HH22OO
HH OHOH
Check Point: 1. Draw the structural formula for C2H4. Remember that each carbon has 4 bonds; each hydrogen has 1.
2.When two molecules of glucose (C6H12O6) are joined together in a dehydration synthesis reaction, what are the formulas of the two products?
CarbohydratesSugars
Monosaccharides: Simple sugars (monomers)
Molecular formula: Multiple of CH2OEx. Glucose and Fructose - C6H12O6
Isomers
Isomers: Same molecular formula, different structure and therefore different properties
Disaccharides: double sugar
Table Sugar
High Fructose Corn Syrup: Corn syrup producers developed a way to convert half of the glucose in corn
syrup to fructose (sweeter)
Polysaccharides: Complex carbohydrates- long chains of sugar units
Starch: Form of stored sugars in plant roots and other plant organs**Potatoes, wheat, rice, and corn are high in starch
bioweb.wku.edu
Glycogen: Form of stored sugars in animals, found in liver and muscle
cells.
Cellulose: Structural component of plants, found in the cell walls. Unable to be digested by animals. (Fiber)
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Lipids (C, H, O)
Nonpolar – don’t dissolve in water–hydrophobic- water fearing.
High proportion of C-H bondsvery little O (oxygen)Some lipids may contain P and NNot polymers
13
LipidsG
lyce
rol
Fatty acid
•Fats, Oils, and Waxes
•Stores energy (2x as much as carbs)
•Stored in adipose cells
Fatty acid
Fatty acid
Triglyceride}
Lipids•Fats, Oils, and Waxes
•Stores energy (2x as much as carbs)
•Stored in adipose cells
Composed of 1 glycerol and 3 fatty acid molecules joined
by dehydration synthesis
Fat = Triglyceride
Glycerol 3 Fatty Acid Chains
Saturated v. Unsaturated Fats•Saturated: When all 3 fatty acid chains
are bonded to the maximum number of hydrogens (No Double Bonds)
•Unsaturated: When at least one fatty acid chain has less then the maximum number of hydrogens (At least one double bond)
Monounsaturated Fat Molecule
Steroids•Hydrophobic
•Cholesterol: Present in cell membrane and is base molecule for other steroids in the body such as testosterone and estrogen
Cholesterol
Anabolic Steroids: synthetic variants of testosterone
Used to build muscle quickly and increase performance
Risks: - Increase cholesterol - Infertility
http://www.muscleenhancers.com/steroids/
Proteins•Types of Proteins:
•Structural (hair, webs)
•Storage (seeds)
•Contractile (muscles)
•Transport (hemoglobin)
•Defensive (antibodies)
•Signal
•Enzymes (lactase)
Monomers = Amino Acids
http://www.aloeveraibs.com/aloe-vera-vitamins
http://universe-review.ca/F11-monocell.htm
*** Each “R” group is unique and determines the chemical properties of the amino acid
20 different amino acids!
Protein Polymers
•A Polypeptide is formed when dehydration synthesis results in peptide bonds between many amino acids
How do we make all of the tens of thousand different polypeptides in our bodies from
only 20 different amino acids?
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Functions of Proteins
Enzymes: regulate the rate of chemical reactions in cells. – eg: Catalysts - speed up or slow down
Structural Proteins – – Viruses - outer coat, – keratin (hair, nails, hoofs, horns)– Collagen -extra cellular matrix (ex. tendons, cartilage)
Hormones- (signaling) Oxytocin, Insulin, Vasopressin
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Functions of Proteins
• Contractile proteins – Actin, Myosin
• Storage Proteins – Casein (nutrient storage in milk), Ferritin (iron
storage in egg yolk and spleen)
• Transport Proteins – Hemoglobin, serum albumin (carries fatty acids
in blood)
• Immunological Proteins – Gamma globulins (circulating antibodies)
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Protein continued
Shape important– “Hydrogen bonds”-help dictate shape
– side groups (R) interact along the polypeptide chain• Causing:
–coil = spiral staircase, phone cord–Folding = Pleated sheet–combo -
– The shape: coil, stretched out, or folded• Determines how a protein will act…(function)
Primary Structure: The amino acid sequence of a protein (Usually at least 100 amino acids long)
Campbell
nature.com
isbbio2.wikispaces.com
Secondary Structure: Hydrogen Bonds between amino acids groups lead to patterns. Patterns are either alpha helix or beta pleated sheets
Quarternary Structure: When a protein consists of more than one polypeptide chain
bonding with one another
yellowtang.org
Ex: Hemoglobin
What determines protein structure?
•The amino acids sequence determines the shape and therefore the function of each protein.
•The shape of a protein allows it to carry on it’s specific function. If it loses it’s shape it will not work correctly.
•Unfavorable pH and temperature can cause denaturation (unfolding) of a protein and cause it to cease functioning normally until pH or temperature returns to normal.
•Metabolism: All of the chemical reactions that occur in an organism
•ENZYMES: Specialized PROTEINS that allow reactions to occur
•Enzymes speed up chemical reactions
Activation Energy: Energy needed to activate reactants and trigger a chemical reaction
For a chemical reaction to occur the bonds in the reactants must be broken which requires the molecules to absorb energy.
Enzymes reduce the amount of activation
energy required to break the bonds in the reactant
molecules
Induced Fit* Enzymes can also be referred
to as catalystsEach enzyme is specific as to which
reactions it catalyzes
Enzymes are proteins, and just like other proteins they need to be the correct shape
to perform their function correctly.
•Substrate: The reactant molecule that interacts with the protein
•Active Site: The area of the enzyme that interacts with the substrate. The shape and chemistry of it allows it to interact with the substrate.
•Induced fit: When the substrate slips into the active site the active site changes its shape slightly to allow a better fit.
When the product is released the enzyme is free to work again. (Catalysts are not used up
in reaction!)
Enzyme Inhibitors
•Inhibit metabolic reactions by binding to an enzyme and disrupting its function
•2 types
2. Bind to some place other than active site, changing the shape of the enzyme making active site no longer the correct
shape to bind to the substrate
Feedback Regulation: If metabolism produces more of a certain product than is needed the product may inhibit the enzyme required for its own production
**Saves Resources
Nucleic AcidsInformation storing molecules that hold
instructions for protein building
DNA and RNA(Genetic Material
Nucleic Acids are polymers of monomers called nucleotides
Nucleotides: Made up of 3 parts1. 5 Carbon Sugar (Deoxyribose or Ribose)2. Phosphate Group3. Nitrogenous Base - (Adenine, Thymine, Guanine, Cytosine, Uracil)
biologyjunction.com
msu.edu