Protein Backbone Dynamics through 13C‘−13Cα Cross-Relaxation in NMR Spectroscopy
- 1 August 2006
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 128 (34) , 11072-11078
- https://doi.org/10.1021/ja0600577
Abstract
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 2Nz and 2Nz . This amounts to “anchoring” the and operators to the Nz 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.Keywords
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