Weak alignment NMR: a hawk-eyed view of biomolecular structure.

Printer-friendly versionPrinter-friendly versionPDF versionPDF version
TitleWeak alignment NMR: a hawk-eyed view of biomolecular structure.
Publication TypeJournal Article
Year of Publication2005
AuthorsBax, A, Grishaev, A
JournalCurr Opin Struct Biol
Volume15
Issue5
Pagination563-70
Date Published2005 Oct
ISSN0959-440X
KeywordsAnimals, Anisotropy, Computer Simulation, Humans, Models, Molecular, Nuclear Magnetic Resonance, Biomolecular, Protein Conformation, Proteins, Ubiquitin
Abstract

Imposing a very slight deviation from the isotropic random distribution of macromolecules in solution in an NMR sample tube permits the measurement of residual internuclear dipolar couplings (RDCs). Such interactions are very sensitive functions of the time-averaged orientation of the corresponding internuclear vectors and thereby offer highly precise structural information. In recent years, advances have been made both in the technology to measure RDCs and in the computational procedures that integrate this information in the structure determination process. The exceptional precision with which RDCs can be measured under weakly aligned conditions is also starting to reveal the mostly, but not universally, subtle effects of internal protein dynamics. Importantly, RDCs potentially can reveal motions taking place on a timescale slower than rotational diffusion and analysis is uniquely sensitive to the direction of motion, not just its amplitude.

DOI10.1016/j.sbi.2005.08.006
Alternate JournalCurr. Opin. Struct. Biol.
PubMed ID16140525
Grant List / / Intramural NIH HHS / United States