Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Convection compensated electrophoretic NMR
Autore:
He, QH; Wei, ZH;
Indirizzi:
Univ Connecticut, Dept Chem, Storrs, CT 06269 USA Univ Connecticut StorrsCT USA 06269 cut, Dept Chem, Storrs, CT 06269 USA Univ Connecticut, Dept Comp Sci & Engn, Storrs, CT 06269 USA Univ Connecticut Storrs CT USA 06269 omp Sci & Engn, Storrs, CT 06269 USA
Titolo Testata:
JOURNAL OF MAGNETIC RESONANCE
fascicolo: 2, volume: 150, anno: 2001,
pagine: 126 - 131
SICI:
1090-7807(200106)150:2<126:CCEN>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
NUCLEAR-MAGNETIC-RESONANCE; DIFFUSION-COEFFICIENTS; ELECTROLYTE-SOLUTIONS; TRANSFERENCE NUMBERS; ELECTRIC-CURRENT; MOBILITY; SPECTROSCOPY; MIXTURES; DESIGN; VELOCITIES;
Keywords:
electrophoretic NMR; pulsed field gradient; flow and convection compensation; structure characterization of protein interactions;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Physical, Chemical & Earth Sciences
Citazioni:
28
Recensione:
Indirizzi per estratti:
Indirizzo: He, QH Mem Sloan Kettering Canc Ctr, Dept Med Phys, 1275 York Ave, New York, NY 10021 USA Mem Sloan Kettering Canc Ctr 1275 York Ave New York NY USA 10021 SA
Citazione:
Q.H. He e Z.H. Wei, "Convection compensated electrophoretic NMR", J MAGN RES, 150(2), 2001, pp. 126-131

Abstract

A novel method of convection compensated ENMR (CC-ENMR) has been developedto detect electrophoretic motion of ionic species in the presence of bulk solution convection. This was accomplished using a gradient moment nulling technique to remove spectral artifacts from heat-induced convection and using the polarity switch of the applied electric field to retain spin phase modulations due to electrophoretic flow. Experiments were carried out with amixture of 100 mM L-aspartic acid and 100 mM 4,9-dioxa-1,12-dodecanediamine to demonstrate this new method of ENMR. CC-ENMR enhances our previously developed capillary array ENMR (CA-ENMR) in solving the convection problem. The combined CA- and CC-ENMR approach strengthens the potential of multidimensional ENMR in simultaneous structural determination of coexisting proteins and protein conformations in biological buffer solutions of high ionic strength. Structural mapping of interacting proteins during biochemical reactions becomes possible in the future using ENMR techniques, which may have a profound impact on the understanding of biological events, including protein folding, genetic control, and signal transduction in general. (C) 2001 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/05/20 alle ore 04:50:00