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Determination of the spatial structure of glutathione by residual dipolar coupling analysis

โœ Scribed by Anton V. Klochkov; Bulat I. Khairutdinov; Murat S. Tagirov; Vladimir V. Klochkov

Publisher
John Wiley and Sons
Year
2005
Tongue
English
Weight
107 KB
Volume
43
Category
Article
ISSN
0749-1581

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โœฆ Synopsis

Abstract

The approach based on analysis of the residual ^1^H๏ฃฟ^13^C dipolar couplings in molecules partially aligned in a lyotropic liquid crystalline medium was used in the NMR investigation of the reduced glutathione (Gluโ€“Cysโ€“Gly; GSH) structure in a lyotropic medium (cetylpyridinium chlorideโ€“nโ€hexanol). The spatial structure of GSH in solution was established on the basis of the experimental data for observed couplings only. Copyright ยฉ 2005 John Wiley & Sons, Ltd.

๐Ÿ“œ SIMILAR VOLUMES

Spatial structure of peptides determined
Spatial structure of peptides determined by residual dipolar couplings analysis
โœ Vladimir V. Klochkov; Roustem F. Baikeev; Vladimir D. Skirda; Anton V. Klochkov; ๐Ÿ“‚ Article ๐Ÿ“… 2009 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 209 KB

## Abstract The gated decoupled ^13^C NMR spectra of a dipeptide (Gluโ€Trp) and a tetrapeptide (NAcโ€Serโ€Pheโ€Valโ€Glyโ€OMe) were recorded in D~2~O and in a lyotropic alignment medium (pentaethylene glycol monododecyl ether/__n__โ€hexanol). The residual dipolar couplings were extracted as the differences