Dipolar couplings as a probe of molecular dynamics and structure in solution.
The introduction of residual dipolar coupling methodology has increased the scope of structural biological problems that can be addressed by NMR spectroscopy. Conformational changes, the relative orientation of domains, and intermolecular complexes can now be characterized accurately and rapidly using NMR. The development of residual dipolar coupling methodology for the rapid recognition of homologous protein folds and for studies of submillisecond timescale dynamics has also seen considerable progress.
Tolman
J R
JR
Section de Chimie, BCH, Université de Lausanne, Switzerland. joel.tolman@icma.unil.ch
D046911:Macromolecular Substances; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D012996:Solutions; D013816:Thermodynamics
D046911:Macromolecular Substances; D011506:Proteins; D012996:Solutions