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Origin of the Residual NMR Linewidth of a Peptide Bound to a Resin under Magic Angle Spinning

✍ Scribed by Karim Elbayed; Maryse Bourdonneau; Julien Furrer; Thierry Richert; Jésus Raya; Jérôme Hirschinger; Martial Piotto

Publisher
Elsevier Science
Year
1999
Tongue
English
Weight
42 KB
Volume
136
Category
Article
ISSN
1090-7807

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✦ Synopsis

The tetrapeptide Ala-lle-Gly-Met bound to a Wang resin via the methionine residue was studied by NMR under MAS conditions and compared to the same peptide in solution. The bound peptide exhibits average linewidths superior to those observed for the peptide in solution. The origin of the residual NMR linewidth observed for the bound form was investigated. The dynamics of the peptide is shown to be only marginally responsible for the increased linewidth; the major cause of the line broadening appears to be nonaveraged magnetic susceptibility differences.

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