Biochemistry 2280A Lecture Notes - Lecture 3: Equilibrium Constant, Ribosome, Proteasome
14 Dec 2016
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Document Summary
De ne and describe tertiary and quaternary structure. Be able to describe a protein domain"s characteristics. Learn how proteins fold and how they become unfolded. Be able to list different functions of proteins. Understand what ligands are and how they bind to proteins. Understand the concept of dissociation constant (kd) De nition: distinct region of a protein: domains can often fold independently, domains provide structure and/or function. Many proteins made up of connected domains. Related domains often found in different proteins: evolution has mixed and matched" domains. Many proteins consist of more than one polypeptide. Forces/bonds involved are the same as for 3 : hydrophobic, h-bonds, van der waals, ionic, disul de bonds. Phosphorylation, ubiquitination, acetylation, sumoylation alters stability or signalling. Folding pathways likely are speci ed by sequence. Molecular chaperons are proteins that help with folding. Probably a stepwise process: hydrophobic interactions, then 2 structure, then 3 . Various types of motion possible depending on structure.
