Observation of noncooperative folding thermodynamics in simulations of 1BBL.

ABSTRACT: One of the predictions of the energy landscape theory of protein folding is the possibility of barrierless, "downhill" folding under certain conditions. The protein 1BBL has been proposed to fold by such a downhill mechanism, though this is a matter of some dispute. We carried out extensive replica exchange molecular dynamics simulations on 1BBL in explicit solvent to address this controversy and provide a microscopic picture of its folding thermodynamics. Our simulations show two distinct structural transitions in the folding of 1BBL. A low-temperature transition involves a disordering of the protein's tertiary structure without loss of secondary structure. A distinct, higher temperature transition involves the complete loss of secondary structure and dissolution of the hydrophobic core.

SUBMITTER: Pitera JW 

PROVIDER: S-EPMC2397362 | biostudies-literature | 2008 Jun

REPOSITORIES: biostudies-literature