Spatial structure of peptides determined by residual dipolar couplings analysis

✍ Scribed by Vladimir V. Klochkov; Roustem F. Baikeev; Vladimir D. Skirda; Anton V. Klochkov; Farhat R. Muhamadiev; Igor Baskyr; Stefan Berger

• Publisher: John Wiley and Sons
• Year: 2009
• Tongue: English
• Weight: 209 KB
• Volume: 47
• Category: Article
• ISSN: 0749-1581
• DOI: 10.1002/mrc.2349

✦ Synopsis

Abstract

The gated decoupled ^13^C NMR spectra of a dipeptide (Glu‐Trp) and a tetrapeptide (NAc‐Ser‐Phe‐Val‐Gly‐OMe) were recorded in D~2~O and in a lyotropic alignment medium (pentaethylene glycol monododecyl ether/n‐hexanol). The residual dipolar couplings were extracted as the differences between the observed couplings for the magnetic nuclei dissolved in the latter and former media. Using a computational optimization, the spatial structures of the compounds were calculated starting from their respective low energy conformations obtained on a semiempirical basis. The uniformity of each conformation was confirmed by the solid‐state ^13^C NMR spectra of powder samples. Differences between the starting structures and final ones, optimized when employing residual dipolar couplings, are discussed. Copyright © 2008 John Wiley & Sons, Ltd.