The inverted free energy landscape of an intrinsically disordered peptide by simulations and experiments.

ABSTRACT: The free energy landscape theory has been very successful in rationalizing the folding behaviour of globular proteins, as this representation provides intuitive information on the number of states involved in the folding process, their populations and pathways of interconversion. We extend here this formalism to the case of the Aβ40 peptide, a 40-residue intrinsically disordered protein fragment associated with Alzheimer's disease. By using an advanced sampling technique that enables free energy calculations to reach convergence also in the case of highly disordered states of proteins, we provide a precise structural characterization of the free energy landscape of this peptide. We find that such landscape has inverted features with respect to those typical of folded proteins. While the gl

SUBMITTER: Granata D 

PROVIDER: S-EPMC4620491 | biostudies-literature | 2015 Oct

REPOSITORIES: biostudies-literature