Effects of macromolecular crowding on an intrinsically disordered protein

Abstract

Proteins are composed of amino acids, and usually have one native structure. Intrinsically disordered proteins lack a native structure and can populate many different forms, making them ideal for binding. My project is to develop a coarse-grained computational model of an IDP known as ⍺-synuclein, which is found in the brains of Parkinson's disease patients. ⍺-synuclein is an 140 amino acid length protein, and will be modeled using Langevin Dynamics. The free parameters of the model are determined by matching the size of the protein chain, as quantified by the radius of gyration