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Side-chain conformation and dynamics in a solid peptide: CP-MAS NMR study of valine rotamers and methyl-group relaxation in fully 13C-labelled antamanide

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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.

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Straus, S.K., Bremi, T. & Ernst, R.R. Side-chain conformation and dynamics in a solid peptide: CP-MAS NMR study of valine rotamers and methyl-group relaxation in fully 13C-labelled antamanide. J Biomol NMR 10, 119–128 (1997). https://doi.org/10.1023/A:1018376516116

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