Dataset Information


Transition-path sampling of beta-hairpin folding.

ABSTRACT: We examine the dynamical folding pathways of the C-terminal beta-hairpin of protein G-B1 in explicit solvent at room temperature by means of a transition-path sampling algorithm. In agreement with previous free-energy calculations, the resulting path ensembles reveal a folding mechanism in which the hydrophobic residues collapse first followed by backbone hydrogen-bond formation, starting with the hydrogen bonds inside the hydrophobic core. In addition, the path ensembles contain information on the folding kinetics, including solvent motion. Using the recently developed transition interface sampling technique, we calculate the rate constant for unfolding of the protein fragment and find it to be in reasonable agreement with experiments. The results support the validation of using all-atom force fields to study protein folding.


PROVIDER: S-EPMC218724 | BioStudies | 2003-01-01

REPOSITORIES: biostudies

Similar Datasets

2005-01-01 | S-EPMC1305027 | BioStudies
2011-01-01 | S-EPMC3131341 | BioStudies
2019-01-01 | S-EPMC6581425 | BioStudies
2001-01-01 | S-EPMC64961 | BioStudies
2006-01-01 | S-EPMC2242415 | BioStudies
2015-01-01 | S-EPMC4379956 | BioStudies
2010-01-01 | S-EPMC2820652 | BioStudies
2010-01-01 | S-EPMC2920744 | BioStudies
2008-01-01 | S-EPMC2567936 | BioStudies
2013-01-01 | S-EPMC3740565 | BioStudies