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Updated: Jun 28, 2026

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
Published on: December 16, 2013
Spatial structure of peptides determined by residual dipolar couplings analysis
Vladimir V Klochkov1, Roustem F Baikeev, Vladimir D Skirda
1Department of Physics, Kazan State University, Kazan, Russian Federation.
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.
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