Amino Acids & Proteins The Molecules in Cells Ch 3.
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Transcript of Amino Acids & Proteins The Molecules in Cells Ch 3.
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Amino Acids & Proteins
The Molecules in CellsCh 3
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Overview of Protein Function
Proteins are involved in cellular structure movement defense transport communication catalysis (enzymes) regulation
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Protein
Mammalian hair is composed of structural proteins
Proteins have a broad size range RNA digesting enzyme ribonuclease A
(molecular weight of 5733 and 51 amino acids long)
Cholesterol transport protein apolipoprotein B (molecular weight of 513,000 and 4636 amino acids long)
Enzymes regulate chemical reactions
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Proteins
Made from 20 different amino acids Proteins are the most structurally and
functionally diverse of life’s molecules Their diversity is based on different
arrangements of amino acids
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Amino Acid Structure
Amino Group Carboxyl Group
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Amino Acid Structure
Each amino acid contains: an amino group a carboxyl group an R group, which distinguishes each of
the 20 different amino acids Each amino acid has specific chemical
properties
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Properties of Amino Acids
Determined by the R group Amino acids may be:
Non-polar Neutral, polar Positively charged, polar Negatively charged, polar
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Properties of Amino Acids
Leucine (Leu)
HYDROPHOBIC
Serine (Ser) Cysteine (Cys)
HYDROPHILIC
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Protein Synthesis: Amino acids can be linked by peptide bonds
A protein is a chain of amino acids linked by peptide bonds
Peptide bond Type of covalent bond Links amino group of one amino acid with
carboxyl group of next Forms through dehydration synthesis reaction
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Peptide Bond Formation
Amino acid Amino acid
PEPTIDEBOND
Dehydration Synthesis Reaction
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Primary Structure of Proteins
A protein’s primary structure is its amino acid sequence
Unique for each protein Two linked amino acids = dipeptide Three or more = polypeptide
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Primary Structure & Protein Shape
Primary structure influences shape in two main ways: Allows hydrogen bonds to form between
different amino acids along length of chain
Puts R groups in positions that allow them to interact
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Protein Shapes
Fibrous proteins Polypeptide chains arranged as strands or
sheets
Globular proteins Polypeptide chains folded into compact, rounded
shapes
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Secondary Structure of Proteins
Hydrogen bonds form between different parts of polypeptide chain
These bonds give rise to coiling or folding pattern
Helix or pleated sheet
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Examples of Secondary Structure
Alpha helix
Pleated sheet
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Tertiary Structure of Proteins
Folding as a result of interactions between R groups
coiled and twisted polypeptide chain of one globin molecule
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Quaternary Structure of Proteins
Some proteins are made up of more than one polypeptide chain
Hemoglobin
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Polypeptides With Attached Organic Compounds
Lipoproteins
Proteins combined with cholesterol, triglycerides,
phospholipids
Glycoproteins
Proteins combined with oligosaccharides
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Denaturation
Disruption of three-dimensional shape Breaking of weak bonds Causes of denaturation:
pH Temperature Salinity
Destroying protein shape disrupts function
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In review ….
What are the similarities & differences between amino acids?
Describe each type of protein structure.
How does shape influence protein function?