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Titolo:
ARGININE SIDE-CHAIN ASSIGNMENTS IN UNIFORMLY N-15-LABELED PROTEINS USING THE NOVEL 2D HE(NE)HGHH EXPERIMENT
Autore:
PELLECCHIA M; WIDER G; IWAI H; WUTHRICH K;
Indirizzi:
ETH HONGGERBERG,INST MOL BIOL & BIOPHYS CH-8093 ZURICH SWITZERLAND
Titolo Testata:
Journal of biomolecular NMR
fascicolo: 2, volume: 10, anno: 1997,
pagine: 193 - 197
SICI:
0925-2738(1997)10:2<193:ASAIUN>2.0.ZU;2-A
Fonte:
ISI
Lingua:
ENG
Soggetto:
PULSED-FIELD GRADIENTS; COUPLING-CONSTANTS; NMR-SPECTRA; RESONANCES; N-15; SENSITIVITY; SEQUENCE; SCHEME; H-1;
Keywords:
NMR ASSIGNMENTS OF ARGININE; PROTEIN STRUCTURE DETERMINATION; PROTEIN-DNA RECOGNITION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
16
Recensione:
Indirizzi per estratti:
Citazione:
M. Pellecchia et al., "ARGININE SIDE-CHAIN ASSIGNMENTS IN UNIFORMLY N-15-LABELED PROTEINS USING THE NOVEL 2D HE(NE)HGHH EXPERIMENT", Journal of biomolecular NMR, 10(2), 1997, pp. 193-197

Abstract

A novel 2D NMR experiment, 2D HE(NE)HGHH, is presented for the assignment of arginine side chain H-1 and N-15 resonances in uniformly N-15-labeled proteins. Correlations between H-1(epsilon), H-1(gamma) and H-1(eta) are established on the basis of (3)J(N-15,H-1) heteronuclear scalar coupling constants, and sequence-specific assignments are obtained by overlap of these fragments with H-1(gamma) chemical shifts obtained by assignment procedures starting from the polypeptide backbone. Since guanidino protons exchange quite rapidly with the bulk water, the 2D HE(NE)HGHH pulse scheme has been optimized to avoid saturation and dephasing of the water magnetization during the course of the experiment. As an illustration, arginine side chain assignments are presented for two uniformly N-15-labeled proteins of 7 and 23 kDa molecular weight.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/09/20 alle ore 07:47:13