PHIL 4 Lecture Notes - Lecture 2: Van Der Waals Force, Competitive Inhibition, Solvent
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[hints: your answer should include the levels of protein structure, the types of chemical bonds involved, chaperones, protein-folding diseases including alzheimer"s and sickle cell, and prions. ] Secondary structure: repeating hydrogen bonds along polypeptide backbone, individually weak but collectively gives coils (fibrous) and pleats (globular). Tertiary structure: overall weak but cumulative effect. Nonpolar amino side chains cluster in center of protein, away from water (van der waal) B. incorrect folding incorrect structure changes function, chaperone proteins: actively fold, safe environment. Sixth amino acid valine instead of glutamic acid causes cells to aggregate into chains, clogging small blood vessels and inhibiting blood flow. The 3 dimensional shape of proteins in cells begins at the most basic level of structure which is the primary structure. The primary structure of proteins is essentially its sequence of amino acids that are joined together covalently through polypeptide bonds. The sequence of the amino acids is determined by genes.
