Biochemistry 3381A Chapter Notes - Chapter 6.4-6.5: Tubulin, Allosteric Regulation, Symmetry Operation
9 Oct 2017
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Document Summary
Protein folding diseases, intrinsically disordered proteins (parts of sect. Denaturation: non-covalent forces are broken leads to primary structure proteins, covalent bonds are not affected, loss of protein structure and function, unfolding is an all-or-none process. Stability: most globular proteins are only marginally stable, this is because we need flexibility in motion. Oligomers complexes composed of non-covalent assemblies of 2 or more monomer subunits: subunits typically fold independently and then interact with the other subunits, can have identical or non-identical subunits. Isologous interactions = interacting surfaces are identical (resulting structure is necessarily dimeric and closed with a 2-fold axis of symmetry: heterologous associations = non-identical interfaces (complementary but not symmetric) Symmetry in quaternary structures: the only symmetry operation possible for protein subunits = rotation. Cyclic subunits are arranged around a single rotation axis (rotating the quaternary structure 180 about this axis gives a structure identical to the original one)
