BIOLOGY 2B03 Lecture Notes - Lecture 2: Ubiquitin Ligase, Groel, Ubiquitin
7 Nov 2013
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Alzheimer"s: most protein molecules fold rapidly into their correct configuration, incompletely folded proteins are assisted in refolding by chaperone proteins, misfolded proteins are recognized for degradation. Prevent improper interaction with other molecules and increase the efficiency of protein folding: molecular chaperones. Selectively bind to hydrophobic amino acids that are exposed in the native non-conformation, allowing it to fold correctly by preventing the developing polypeptide from associating w/ other proteins or folding prematurely. Large cylindrical macromolecule assemblies composed of many proteins: ex. Tcip in cytosol, groel in bacteria/chloroplast, hsp 60 in mitochondria. Form isolation chamber for newly synthesized polypeptides that allow them to fold w/o interference from other macromolecules. Groel shifts to relaxed conformation w/ addition groes cap, releasing protein within chamber: atp hydrolyses to adp, this ejects folded protein. Groel complex (in eukaryotes (varies), 8 in bacteria) Intermediate domain acts a hinge allowing each subunit to move relative to each other.
