BIOL 4374 Lecture Notes - Lecture 3: Lysosome, Coiled Coil, Isoleucine
26 Jan 2017
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Document Summary
Proteins polypeptides made of 20 amino acids. Ex: cystic fibrosis transmembrane regulator: motor proteins. Ex: lac repressor: (cid:498)special purpose(cid:499) proteins. Regulates protein folding; elements of secondary structure. Urea can denature proteins after they have folded. Noncovalent bonds aid the folding of proteins: like hydrogen bonds, van der waal interactions, and electrostatic interactions. Hydrophobic interactions also play a large role in protein folding. Molecular chaperones aid folding of peptide chain: occurs in endoplasmic reticulum lumen, bind to nonpolar amino acid side chains to prevent misfolding, bind as homodimers when atp is present. Atp must hydrolyze for chaperone to dissociate. Improper protein folding disease: prions= misfolded proteins that cause other proteins to misfold as well, alzheimer"s= amyloid plaques, huntington"s disease= a lot of cell death in the brain. 20n possibilities for a polypeptide with n amino acids. Not all amino acids occur with same frequency: l, s, k, e are v common, c, w, m are less common.
