Discrete molecular dynamics can predict helical prestructured motifs in disordered proteins.

ABSTRACT: Intrinsically disordered proteins (IDPs) lack a stable tertiary structure, but their short binding regions termed Pre-Structured Motifs (PreSMo) can form transient secondary structure elements in solution. Although disordered proteins are crucial in many biological processes and designing strategies to modulate their function is highly important, both experimental and computational tools to describe their conformational ensembles and the initial steps of folding are sparse. Here we report that discrete molecular dynamics (DMD) simulations combined with replica exchange (RX) method efficiently samples the conformational space and detects regions populating α-helical conformational states in disordered protein regions. While the available computational methods predict secondary structural pr

SUBMITTER: Szollosi D 

PROVIDER: S-EPMC3998973 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature