ISSN:
1573-5001
Keywords:
Solid-state NMR
;
Peptide dynamics
;
Side-chain conformation
;
Methyl-group relaxation;
;
Homonuclear decoupling
;
Stereospecific assignment
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
Notes:
Abstract The effect of the crystal lattice on the side-chain conformation andside-chain dynamics in peptides is investigated by solid-state NMR, using thecyclic decapeptide antamanide as an example. The study takes advantage of the13C assignment of the backbone and side chains based on theresolution-enhanced 2D spin-diffusion spectra by heteronuclear and homonucleardecoupling. The spectra even allow for a stereospecific assignment of theγ-carbons of the valine residue. It is found that the valine side chaincoexists in two static rotamer conformations which have not been observed byX-ray crystallography. In addition, remarkable effects of the crystal packingon the methyl-group rotation frequency are found from 13Crelaxation measurements.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1023/A:1018376516116
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