期刊
JOURNAL OF MAGNETIC RESONANCE
卷 187, 期 2, 页码 352-356出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.jmr.2007.05.002
关键词
SSNMR; CSA; TOBSY; ROCSA; polypeptides; recouplings; fibrils
We demonstrate that the static powder pattern line shape of chemical shift anisotropy (CSA) can be obtained for unresolved carbonyl sites of polypeptides under magic-angle spinning. The CSA interaction is first recoupled at the carbonyl site. The phase factors associated with the CSA recoupling are then transferred to the adjacent a carbon by an isotropic polarization transfer based on scalar spin-spin coupling. Because a carbons of polypeptides are usually better resolved, we can then obtain the CSA static powder pattern line shapes of the carbonyl sites after Fourier transformation in the second dimension. We validate our approach experimentally by measurements on [U-C-13, N-15]-L-alanine, [U-C-13, N-15]-L-valine and prion fibrils with uniform C-13 and N-15 labels on selected residues. 2007 Elsevier Inc. All rights reserved.
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