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
Proton Dipolar Recoupling in Resin-Bound Peptides under High-Resolution Magic Angle Spinning
✍ Scribed by Jésus Raya; Alberto Bianco; Julien Furrer; Jean-Paul Briand; Martial Piotto; Karim Elbayed
- Publisher
- Elsevier Science
- Year
- 2002
- Tongue
- English
- Weight
- 594 KB
- Volume
- 157
- Category
- Article
- ISSN
- 1090-7807
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✦ Synopsis
Rotational resonance and radiofrequency-driven dipolar recoupling (RFDR) experiments have been used to recover the weak proton dipolar interaction present in peptides bound to swollen resins spun at the magic angle. The intensity of the correlation peaks obtained using these sequences is shown to be significantly stronger than the one obtained using the classical NOESY experiment. In addition, it is found that during the relatively long mixing times required to transfer magnetization in such soft materials, the RFDR sequence also achieves magnetization transfer via the scalar J-coupling.
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