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Folding and self-assembly of a small heterotetramer.

ABSTRACT: Designed miniproteins offer a possibility to study folding and association of protein complexes, both experimentally and in silico. Using replica exchange molecular dynamics and the coarse-grain UNRES force field, we have simulated the folding and self-assembly of the heterotetramer BBAThet1, comparing it with that of the homotetramer BBAT1 which has the same size and ???-fold. For both proteins, association of the tetramer precedes and facilitates folding of the individual chains.

SUBMITTER: Yasar F

PROVIDER: S-EPMC3977861 | biostudies-literature | 2014 Mar

REPOSITORIES: biostudies-literature

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Folding and self-assembly of a small heterotetramer.

Yaşar Fatih F Sieradzan Adam K AK Hansmann Ulrich H E UH

The Journal of chemical physics 20140301 10

Designed miniproteins offer a possibility to study folding and association of protein complexes, both experimentally and in silico. Using replica exchange molecular dynamics and the coarse-grain UNRES force field, we have simulated the folding and self-assembly of the heterotetramer BBAThet1, comparing it with that of the homotetramer BBAT1 which has the same size and ββα-fold. For both proteins, association of the tetramer precedes and facilitates folding of the individual chains. ...[more]

PMID: 24628212

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