BCH210H1 Lecture Notes - Lecture 5: Hydrophobicity Scales, Aliphatic Compound, Isomerase

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Classify the 20 aas based on their side chain"s structure. Describe the importance of each different, chemical functional groups found on each residue"s side chain. Deduce the location of an amino acid in the folded structure of a polypeptide chain. Explain how disulfide bonds are formed and their importance for protein structure. Contrast the effect of a chemical modification on an amino acid"s side chain. The 20 aas have distinct side chains that contribute to a protein"s structure. Non-covalent and covalent interactions between the functional groups are important for stability. The interaction of hydrophilic amino acids with water help solubilize some proteins. H-bonds between hydroxyl, carboxyl, thiol, and aas to help with protein stability. H-bonds can also form between aa side chains within a protein"s structure. Hydrophobic interactions can occur between aliphatic and hydrophobic side chains. Salt bridges can form between positively and negatively charged aas. Ionic interactions are important for ligand, cofactor, and/or substrate binding in enzymes.

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