Computational investigation of cold denaturation in the Trp-cage miniprotein.

ABSTRACT: The functional native states of globular proteins become unstable at low temperatures, resulting in cold unfolding and impairment of normal biological function. Fundamental understanding of this phenomenon is essential to rationalizing the evolution of freeze-tolerant organisms and developing improved strategies for long-term preservation of biological materials. We present fully atomistic simulations of cold denaturation of an α-helical protein, the widely studied Trp-cage miniprotein. In contrast to the significant destabilization of the folded structure at high temperatures, Trp-cage cold denatures at 210 K into a compact, partially folded state; major elements of the secondary structure, including the α-helix, are conserved, but the salt bridge between aspartic acid and arginine is los

SUBMITTER: Kim SB 

PROVIDER: S-EPMC4987839 | biostudies-literature | 2016 Aug

REPOSITORIES: biostudies-literature