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Measurement of one-bond 1H-13C, couplings in backbone-labelled proteins

Lookup NU author(s): Professor Steve Homans

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Abstract

NMR dipole-dipole couplings between protein backbone nuclei (1H, 13C, 15N, 1HN,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-13C couplings can be measured simply and with high sensitivity by use of conventional heteronuclear single quantum correlation (HSQC) techniques.

Publication metadata

Author(s): Giesen AW, Bae LC, Barrett CL, Chyba JA, Chaykovsky MM, Cheng MC, Murray JH, Oliver EJ, Sullivan SM, Brown JM, Dahlquist FW, Homans SW

Publication type: Article

Publication status: Published

Journal: Journal of Biomolecular NMR

Year: 2001

Volume: 19

Issue: 3

Pages: 255-260

ISSN (print): 0925-2738

ISSN (electronic): 1573-5001

Publisher: Springer Netherlands

URL: http://dx.doi.org/10.1023/A:1011298531256

DOI: 10.1023/A:1011298531256

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