Ontology highlight
ABSTRACT:
SUBMITTER: Holliday MJ
PROVIDER: S-EPMC5336394 | biostudies-literature | 2017 Feb
REPOSITORIES: biostudies-literature
Holliday Michael Joseph MJ Camilloni Carlo C Armstrong Geoffrey Stuart GS Vendruscolo Michele M Eisenmesser Elan Zohar EZ
Structure (London, England : 1993) 20170112 2
Many protein systems rely on coupled dynamic networks to allosterically regulate function. However, the broad conformational space sampled by non-coherently dynamic systems has precluded detailed analysis of their communication mechanisms. Here, we have developed a methodology that combines the high sensitivity afforded by nuclear magnetic resonance relaxation techniques and single-site multiple mutations, termed RASSMM, to identify two allosterically coupled dynamic networks within the non-cohe ...[more]