Biochemistry 3380G Lecture Notes - Protein Folding, Coiled Coil, Femtometre

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Many proteins consist of more than one polypeptide and are known for possessing a quaternary structure as a result. The forces/bonds involved in quaternary structures are the same as for tertiary structures (hydrophobic, h-bonds, van der waals, ionic, disulfide bonds). Subunits are the individual polypeptide chains within a quaternary structure. For example, the p53 tetramer, mutated in about 50% of cancers, is comprised of 4 subunits that form a quaternary structure. A type of quaternary structure is the coiled coil, whose repeating sequence plays a very important role in its structure. With a repeating pattern every 7 resides, helices wrap around one another to minimize exposure of hydrophobic residues to the aqueous environment, leaving what is called a hydrophobic stripe on one side of the helix. Examples of proteins containing the coiled coil structure are eb1, which binds to microtubule ends and gcn4 which is a transcription factor. Biochemists indicate protein structure using three distinct models: wire, ribbon and space-filling.

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