Beta turn propensity and a model polymer scaling exponent identify intrinsically disordered phase-separating proteins
Elisia A. Paiz, Jeffre Allen, John J. Correia, Nicholas C. Fitzkee, Loren E. Hough, Steven T. Whitten
Abstract
valence electron interactions. By this mechanism, β-turns could act as energetically favored nucleation points, which may explain the increased propensity for turns in ID regions (IDRs) utilized biologically for phase separation. Phase-separating IDRs, non-phase-separating IDRs, and folded regions could be distinguished by combining v and β-turn propensity. Finally, we propose a new algorithm, ParSe (partition sequence), for predicting phase-separating protein regions, and which is able to accurately identify folded, disordered, and phase-separating protein regions based on the primary sequence.
Topics & Concepts
ExponentIntrinsically disordered proteinsScalingPhase (matter)ChemistrySequence (biology)Chemical physicsNucleationPhysicsCrystallographyThermodynamicsMathematicsBiochemistryOrganic chemistryGeometryLinguisticsPhilosophyRNA Research and SplicingProtein Structure and DynamicsRNA modifications and cancer