BIOLOGY 2B03 Lecture Notes - Lecture 2: Allosteric Modulator, Fetal Hemoglobin, Spinocerebellar Ataxia
6 Nov 2017
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Correcting misfolding chaperones: most proteins fold rapidly into their native conformation. If a cell is exposed to high temperatures, the cell responds by making more heat shock proteins to refold various proteins in the cell. Folded protein is released and the hsp 70 is ready to bind to another unfolded protein. Large complexes, macromolecular complexes containing many different proteins. Include tcip protein found in the cytosol and the groel found in bacteria and chloroplast organelles. In order to change the shape of the groel chamber, each of the seven hsp60 subunits changes shape. Hsp60 can be seen in the ribbon diagram: groel is closed by the groes lid (relaxed conformation), each hsp60 is bound to atp, and each. Hsp60 protein is in an elongated conformation: the individual behaviour of the subunits lead to the overall chaperonin function. Protein degradation: occasionally proteins don"t fold; unfolded proteins are a risk.
