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

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

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...

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Veröffentlicht in:Journal of biomolecular NMR 2001-03, Vol.19 (3), p.255-260
Hauptverfasser: Giesen, A W, Bae, L C, Barrett, C L, Chyba, J A, Chaykovsky, M M, Cheng, M C, Murray, J H, Oliver, E J, Sullivan, S M, Brown, J M, Dahlquist, F W, Homans, S W
Format: Artikel
Sprache:eng
Schlagworte:
Amino Acids - chemistry
Carbon Isotopes
Hydrogen
Isotopic enrichment
Nitrogen Isotopes
Nuclear Magnetic Resonance, Biomolecular - methods
Ubiquitins - chemistry
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Zusammenfassung: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.
ISSN:0925-2738
1573-5001
DOI:10.1023/A:1011298531256