BIOL 3410 Chapter Notes - Chapter 4, 11, 12: Trypsin, Column Chromatography, Lipid Bilayer

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Chapter 4: the shape and structure of proteins. Proteins fold into a conformation of lowest energy. Can be denatured by treatment with solvents that disrupt the noncovalent interactions. When solvent is removed, the protein often refolds spontaneously, known as renaturation. Tend to form aggregates, many times causing death. Chaperone proteins(molecular chaperones): proteins that assist protein folding in a living cell. These proteins bind to partly folded pp chains and help them progress along the most energetically favorable folding pathway. Found in the protein -keratin, which is abundant in skin and its derivatives such as hair, nails, and horns. Resembles a spiral staircase and can be either right- or left- handed. Handedness not affected if upside-down but is if reflected in a mirror. Generated when single polypeptide chain turns around itself to form a structurally rigid cylinder. H-bond at every 4th aa, (cid:272)o(cid:373)plete e(cid:448)ery 3. 6 aa"s: sheet.

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