BCHM 310 Chapter Notes - Chapter 4.3f: Intrinsically Disordered Proteins, Proline, Conformational Change
1 Nov 2017
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Intrinsically disordered proteins have properties distinct from classical structured proteins. They lack a hydrophobic core, and instead are characterized by high densities of charged amino acid residues such as lys, arg, and glu. Pro residues are also prominent, as they tend to disrupt ordered structures. Intrinsically disordered proteins have a high proportion of charged (k, r, d) and polar uncharged amino acid residues. So intrinsically disordered proteins have no hydrophobic core! Idps can be spacers, insulators, or linkers in larger structures because of their structural disorder and high charge density. Other idps can be scavengers, binding up ions and small molecules in solution and serving as reservoirs or garbage dumps. However, the main function of idps is to facilitate protein interactions. Lack of an ordered structure = functional promiscuity, allowing one protein to interact with multiple partners. Idps can inhibit the action of other proteins by wrapping around their protein targets.
