Internal dynamics of proteins are usually characterized by the analysis of 15N relaxation rates that reflect the motions of NHN vectors. It was suggested a decade ago that additional information on backbone motions can be obtained by measuring cross-relaxation rates associated with intra-residue C′Cα vectors. Here we propose a new approach to such measurements, based on the observation of the transfer between two-spin orders 2NzC′z and 2NzC zα. This amounts to "anchoring" the C′z and Czα operators to the N z term from the amide of the next residue. In combination with symmetrical reconversion, this method greatly reduces various artifacts. The experiment is carried out on human ubiquitin at 284.1 K, where the correlation time is 7.1 ns. The motions of the C′Cα vector appear more restricted than those of the NHN vector.
|Original language||English (US)|
|Number of pages||7|
|Journal||Journal of the American Chemical Society|
|State||Published - Aug 30 2006|
ASJC Scopus subject areas
- Colloid and Surface Chemistry