Conformations of intrinsically disordered proteins are influenced by linear sequence distributions of oppositely charged residues.

ABSTRACT: The functions of intrinsically disordered proteins (IDPs) are governed by relationships between information encoded in their amino acid sequences and the ensembles of conformations that they sample as autonomous units. Most IDPs are polyampholytes, with sequences that include both positively and negatively charged residues. Accordingly, we focus here on the sequence-ensemble relationships of polyampholytic IDPs. The fraction of charged residues discriminates between weak and strong polyampholytes. Using atomistic simulations, we show that weak polyampholytes form globules, whereas the conformational preferences of strong polyampholytes are determined by a combination of fraction of charged residues values and the linear sequence distributions of oppositely charged residues. We quantify the

SUBMITTER: Das RK 

PROVIDER: S-EPMC3746876 | biostudies-literature | 2013 Aug

REPOSITORIES: biostudies-literature