Ontology highlight
ABSTRACT:
SUBMITTER: Zheng W
PROVIDER: S-EPMC3562767 | biostudies-literature | 2013 Jan
REPOSITORIES: biostudies-literature
Zheng Weihua W Schafer Nicholas P NP Wolynes Peter G PG
Proceedings of the National Academy of Sciences of the United States of America 20130114 5
Frustration from strong interdomain interactions can make misfolding a more severe problem in multidomain proteins than in single-domain proteins. On the basis of bioinformatic surveys, it has been suggested that lowering the sequence identity between neighboring domains is one of nature's solutions to the multidomain misfolding problem. We investigate folding of multidomain proteins using the associative-memory, water-mediated, structure and energy model (AWSEM), a predictive coarse-grained pro ...[more]