| Literature DB >> 11330812 |
A W Giesen1, L C Bae, C L Barrett, J A Chyba, M M Chaykovsky, M C Cheng, J H Murray, E J Oliver, S M Sullivan, J M Brown, F W Dahlquist, S W Homans.
Abstract
NMR dipole-dipole couplings between protein backbone nuclei (1H(alpha), 13C(alpha), 15N, 1H(N), 13C') offer enormous scope for the rapid determination of protein global folds. Here, we show that measurement of one-bond splittings in the protein backbone is facilitated by use of protein that is selectively isotopically enriched only in the backbone atoms. In particular, 1H(alpha)-13C(alpha) couplings can be measured simply and with high sensitivity by use of conventional heteronuclear single quantum correlation (HSQC) techniques.Entities:
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Year: 2001 PMID: 11330812 DOI: 10.1023/a:1011298531256
Source DB: PubMed Journal: J Biomol NMR ISSN: 0925-2738 Impact factor: 2.835