BIOL 200 Lecture Notes - Lecture 25: Nuclear Pore, Protein Folding, Non-Covalent Interactions
7 Jun 2016
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Influenza virus hemagglutinin: trimer if identical subunits each composed of an. Macromolecular assemblies: the mrna transcription initiation machinery: can be 20-30 separately synthesized proteins in pre-initiation complex. If there are exposed hydrophobic patches on outside of protein that is an issue folding error. Exposed hydrophobic patches tend to non-specifically stick to each other protein aggregation. Several things happen when you have misfolded protein. Cell can try to refold and correct folding mistake. Spontaneous refolding of a denatured protein is though to be through a folding pathway: same for nascent proteins being synthesized on ribosomes. Hsp70 is a major molecular chaperone that helps newly synthesized proteins follow the correct folding pathway: chaperones bind to exposed hydrophobic residues of nascent polypeptdide, and protect from aggregation until properly folded. Form an unclosed chamber made up of inward facing protein binding subunits that undergo concerted atp-binding/hydrolysis and conformation change. Unsure of mechanism: proteins that go in misfolded have chance of coming out properly folded.
