Evolution of All-Atom Protein Force Fields to Improve Local and Global Properties.

ABSTRACT: Experimental studies on intrinsically disordered and unfolded proteins have shown that in isolation they typically have low populations of secondary structure and exhibit distance scalings suggesting that they are at near-theta-solvent conditions. Until recently, however, all-atom force fields failed to reproduce these fundamental properties of intrinsically disordered proteins (IDPs). Recent improvements by refining against ensemble-averaged experimental observables for polypeptides in aqueous solution have addressed deficiencies including secondary structure bias, global conformational properties, and thermodynamic parameters of biophysical reactions such as folding and collapse. To date, studies utilizing these improved all-atom force fields have mostly been limited to a small set of un

SUBMITTER: Zerze GH 

PROVIDER: S-EPMC7507668 | biostudies-literature | 2019 May

REPOSITORIES: biostudies-literature