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MOLECULAR BIOLOGY (2.4 Proteins (Amino Acids (Amino acids all share a…
MOLECULAR BIOLOGY
2.4 Proteins
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Protein Structure
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Secondary
Beta-pleated sheets occur when the amino acid sequence adopts a directionally-oriented staggered strand conformation
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Tertiary
hydrogen bonds, disulfide bridges, ionic interactions, polar associations, etc.
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Amino Acids
There are 20 different amino acids, essential and non essential.
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These side chains will have distinct chemical properties hence cause the protein to fold and function differently.
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joined together on the ribosome to form polypeptides,
Amino acids all share a common basic structure, with a central carbon atom bound to:
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Peptide Bonds
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Polypeptide chains can be broken down via hydrolysis reactions, which requires water to reverse the process
The covalent bond between the amino acids is called a peptide bond and long chains of covalently bonded amino acids are called polypeptides
Amino acids can be covalently joined together in a condensation reaction to form a dipeptide and water
2.5 Enzymes
Enzyme Catalysis
The enzyme and product then dissociate – as the enzyme was not consumed, it can continue to catalyse further reactions
The enzyme catalyses the conversion of the substrate into product, creating an enzyme-product complex
When a substrate binds to the enzyme’s active site, an enzyme-substrate complex is formed
Enzyme catalysis requires that the substrate be brought into close physical proximity with the active site
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Active Site
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The active site and the substrate complement each other in terms of both shape and chemical properties
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