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Titolo:
H-1 MAGNETIC CROSS-RELAXATION BETWEEN MULTIPLE SOLVENT COMPONENTS ANDROTATIONALLY IMMOBILIZED PROTEIN
Autore:
HINTON DP; BRYANT RG;
Indirizzi:
UNIV VIRGINIA,DEPT CHEM CHARLOTTESVILLE VA 22901 UNIV VIRGINIA,DEPT CHEM CHARLOTTESVILLE VA 22901
Titolo Testata:
Magnetic resonance in medicine
fascicolo: 4, volume: 35, anno: 1996,
pagine: 497 - 505
SICI:
0740-3194(1996)35:4<497:HMCBMS>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
HETEROGENEOUS SPIN SYSTEMS; AQUEOUS-SOLUTION; LONGITUDINAL MAGNETIZATION; SELECTIVE SATURATION; HYDRATED COLLAGEN; PROTON RELAXATION; TRANSIENT DECAY; WATER-MOLECULES; DIFFUSION; EXCHANGE;
Keywords:
CROSS-RELAXATION; MAGNETIZATION TRANSFER; PROTEIN SOLVATION; PREFERENTIAL SOLVATION; Z-SPECTROSCOPY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
45
Recensione:
Indirizzi per estratti:
Citazione:
D.P. Hinton e R.G. Bryant, "H-1 MAGNETIC CROSS-RELAXATION BETWEEN MULTIPLE SOLVENT COMPONENTS ANDROTATIONALLY IMMOBILIZED PROTEIN", Magnetic resonance in medicine, 35(4), 1996, pp. 497-505

Abstract

Magnetic cross-relaxation spectra or Z-spectra are presented for water, acetone, methanol, dimethylsulfoxide, and acetonitrile in cross-linked bovine serum albumin gels. Each solvent studied, reports the same Z-spectrum linewidth and shape for the solid component that follows from solutions of the coupled relaxation equations. The Z-spectra demonstrate competition among solvents for specific protein binding sites. The rate of magnetization transfer in the rotationally immobilized protein environment is approximated by 1/T-2 for the solid component, which is shown to account for the observed magnetization transfer rates inthe systems studied. The temperature dependence of the Z-spectra are different for water compared with the organic solvents. The cross-relaxation efficiency in the organic solvents decreases with increasing temperature because molecules bind less well at high temperature. For water, the hydrogen exchange path becomes increasingly important relative to the whole molecule path with increasing temperature, which improves the net cross-relaxation efficiency.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 08/07/20 alle ore 06:42:23