Biochemistry 2280A Lecture Notes - Lecture 5: Hemeprotein, Metalloprotein, Coiled Coil
12 Dec 2016
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Topic 3 continued: tertiary structure: when a single polypeptide can independently fold into shapes. Domain: individual region that can independently form it"s own little cluster. Multiple domains within one polypeptide: quaternary structure: more than one polypeptide! Many proteins consist of more than one polypeptide. Within each of the subunits, there can be domains. The forces/bonds that are involved are the same as for the tertiary structure. Hydrophobic, h-bonds, van der waals, ionic, disulfide bonds: quaternary structure: coiled coil . Two polypeptides that are wrapped around each other. There"s a strip of hydrophobic amino acid residues along each polypeptide. Since hydrophobic residues like to stick together, they wrap around each other becoming the inside , and then the coiled coil is the outside : indicating protein structure. Shows which amino acids are on the surface. Predict interactions with water or proteins: post-translational modifications. After it"s translated, it can be phosphorylated, acetylated or ubiquinated as well.
