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- W2034891005 abstract "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." @default.
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- W2034891005 date "2008-10-21" @default.
- W2034891005 modified "2023-09-30" @default.
- W2034891005 title "Spatial structure of peptides determined by residual dipolar couplings analysis" @default.
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- W2034891005 doi "https://doi.org/10.1002/mrc.2349" @default.
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