Ontology highlight
ABSTRACT:
SUBMITTER: De Simone A
PROVIDER: S-EPMC3236604 | biostudies-literature | 2011 Dec
REPOSITORIES: biostudies-literature
De Simone Alfonso A Montalvao Rinaldo W RW Vendruscolo Michele M
Journal of chemical theory and computation 20111010 12
In order to carry out their functions, proteins often undergo significant conformational fluctuations that enable them to interact with their partners. The accurate characterization of these motions is key in order to understand the mechanisms by which macromolecular recognition events take place. Nuclear magnetic resonance spectroscopy offers a variety of powerful methods to achieve this result. We discuss a method of using residual dipolar couplings as replica-averaged restraints in molecular ...[more]