Ontology highlight
ABSTRACT:
SUBMITTER: Tarakanova A
PROVIDER: S-EPMC6048532 | biostudies-literature | 2018 Jul
REPOSITORIES: biostudies-literature
Tarakanova Anna A Yeo Giselle C GC Baldock Clair C Weiss Anthony S AS Buehler Markus J MJ
Proceedings of the National Academy of Sciences of the United States of America 20180626 28
Protein folding poses unique challenges for large, disordered proteins due to the low resolution of structural data accessible in experiment and on the basis of short time scales and limited sampling attainable in computation. Such molecules are uniquely suited to accelerated-sampling molecular dynamics algorithms due to a flat-energy landscape. We apply these methods to report here the folded structure in water from a fully extended chain of tropoelastin, a 698-amino acid molecular precursor to ...[more]