Hydropathy Patterning Complements Charge Patterning to Describe Conformational Preferences of Disordered Proteins

• DOI: 10.1021/acs.jpclett.0c00288
• Publication Date: 2020-03-31T23:46:36Z
• Authors: Wenwei Zheng; Gregory Dignon; Matthew Brown; Young C. Kim; Jeetain Mittal
• Keywords: Intrinsically Disordered Proteins; Sequence (biology)

Understanding the conformational ensemble of an intrinsically disordered protein (IDP) is great interest due to its relevance critical intracellular functions and diseases. It now well established that polymer scaling behavior can provide a deal information about properties as liquid–liquid phase separation IDP. is, therefore, extremely desirable be able predict IDP's from sequence itself. The work in this direction so far has focused on highly charged proteins how charge patterning perturb their structural properties. As naturally occurring IDPs are composed significant fraction uncharged amino acids, rules based content only partially helpful solving problem. Here, we propose new order parameter, hydropathy decoration, which near-quantitative understanding devoid residues. We combine with obtain general equation, parametrized extensive coarse-grained simulation data, for predicting dimensions sequence. finally test equation against available experimental data find semiquantitative match behavior. also guidance extend approach should feasible near future.