BIOL 200 Lecture Notes - Lecture 5: Hsp60, Protein Folding, Conformational Change
20 Sep 2019
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And they have to do it with the shape of the proteins. They work through atp-dependent cycles of binding to, and release from misfolded client molecules. The molecules that are misfolded are called client . The binding is at exposed hydrophobic patches. The signal that tells the chaperone that the protein needs help / it is misfolded: the hydrophobic part is on the outside with water/cytoplasm (it supposed to be interacting with other hydrophobic molecule) The chaperone blocks the exposed hydrophobic patches and therefore, keeps the folding or refolding protein out of trouble until the proper folding occurs. There are two major classes of chaperone: molecular chaperones operate as a single molecule, chaperonins form a multisubunit refolding chamber, an organelle essentially. Hsp 70 is a major molecular chaperone (heat-shock proteins) It helps newly-synthesized proteins follow the correct folding pathway. They work on nascent protein (synthesized on a ribosome) or unfolded protein.
