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Titolo:
Magnetization transfer from laser-polarized xenon to protons located in the hydrophobic cavity of the wheat nonspecific lipid transfer protein
Autore:
Landon, C; Berthault, P; Vovelle, F; Desvaux, H;
Indirizzi:
CEA Saclay, Serv Chim Mol, Lab Commun RMN, F-91191 Gif Sur Yvette, France CEA Saclay Gif Sur Yvette France F-91191 F-91191 Gif Sur Yvette, France CNRS, Ctr Biophys Mol, F-45071 Orleans 02, France CNRS Orleans France 02CNRS, Ctr Biophys Mol, F-45071 Orleans 02, France
Titolo Testata:
PROTEIN SCIENCE
fascicolo: 4, volume: 10, anno: 2001,
pagine: 762 - 770
SICI:
0961-8368(200104)10:4<762:MTFLXT>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
CRYSTAL-STRUCTURE; PHAGE-T4 LYSOZYME; DETECT WATER; NOBLE-GASES; NMR; BINDING; MAIZE; ENHANCEMENT; MOLECULES; EXCHANGE;
Keywords:
laser-polarized xenon; SPINOE; wheat nonspecific lipid transfer protein; protein hydrophobic cavity;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
47
Recensione:
Indirizzi per estratti:
Indirizzo: Desvaux, H CEA Saclay, Serv Chim Mol, Lab Commun RMN, F-91191 Gif Sur Yvette, France CEA Saclay Gif Sur Yvette France F-91191 f Sur Yvette, France
Citazione:
C. Landon et al., "Magnetization transfer from laser-polarized xenon to protons located in the hydrophobic cavity of the wheat nonspecific lipid transfer protein", PROTEIN SCI, 10(4), 2001, pp. 762-770

Abstract

Nonspecific lipid transfer protein from wheat is studied by liquid-state NMR in the presence of xenon. The gas-protein interaction is indicated by the dependence of the protein proton chemical shifts on the xenon pressure and formally confirmed by the first observation of magnetization transfer from laser-polarized xenon to the protein protons. Twenty-six heteronuclear nOes have allowed the characterization of four interaction sites inside the wheat ns-LTP cavity, Their locations are in agreement with the variations ofthe chemical shifts under xenon pressure and with solvation simulations. The richness of the information obtained by the noble gas with a nuclear polarization multiplied by similar to 12,000 makes this approach based on dipolar cross-relaxation with laser-polarized xenon promising for probing protein hydrophobic pockets at ambient pressure.

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Documento generato il 06/04/20 alle ore 02:15:44