BIOLOGY 2B03 Lecture 2: Module 2
15 Jan 2016
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Document Summary
Bind to hydrophobic aa residues/r groups to prevent misfolding, premature folding and aggregation with other hydrophobic residues via hydrophobic interactions. Hsp70 atpase cycle: both unfolded or nascent (leaving ribosome) protein have a hydrophobic patch (of hydrophobic residues) that bind to the hsp70 rapidly, co chaperone dnaj/hsp40 hydrolyzes atp to adp, atp hydrolysis hsp70 changes conformation change in shape of protein, that helps stimulate accurate folding, hsp70 releases adp, with help by grpe/bag1, new atp binds to nucleotide binding domain release folded protein. Found in cytosol (tcip) and bacteria and chloroplast (groel: top chamber: binds to atp and new peptide. 8: ubiquitinylation, e1 recognizes free ubiquitin in cytosol and binds to it (atp hydrolysis, proteins taken up into the cell, regulated proteins, e1: ubiquitin activating enzyme, ubiquitin is transferred to e2, e2: ubiquitin conjugating enzyme, e3 recognizes and picks up the target protein, e3: ubiquitin ligase; large family of proteins in which each member recognizes a different signal.
