Dynamic and magnetic susceptibility effects on the MAS NMR linewidth of a tetrapeptide bound to different resins
| Autor: | Julien Furrer, Alberto Bianco, David Limal, Maryse Bourdonneau, Karim Elbayed, Jésus Raya, Martial Piotto |
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| Rok vydání: | 2002 |
| Předmět: |
animal structures
Tetrapeptide Carbon-13 NMR satellite Chemistry technology industry and agriculture Analytical chemistry General Chemistry Nuclear magnetic resonance spectroscopy Fluorine-19 NMR Carbon-13 NMR Magnetic susceptibility Crystallography embryonic structures Magic angle spinning Proton NMR General Materials Science |
| Zdroj: | Magnetic Resonance in Chemistry. 40:123-132 |
| ISSN: | 1097-458X 0749-1581 |
| DOI: | 10.1002/mrc.970 |
| Popis: | Under magic angle spinning, the NMR spectrum of the tetrapeptide Ala-Ile-Gly-Met bound to a Wang resin, and swollen in DMF, exhibits proton and carbon linewidths that are sharp enough to allow the complete characterization of the peptide using classical liquid-state NMR methods. The proton linewidths of the bound peptide remain, however, about three times larger than those of the free peptide in solution. The residual NMR linewidth originates essentially from incompletely averaged magnetic susceptibility effects due to the Wang resin. Replacing the aromatic Wang resin with a PEGA or POEPOP resin removes this effect. To investigate the contribution to line broadening of the peptide dynamics, relaxation studies were performed on the peptide bound to Wang and POEPOP resins. Copyright © 2001 John Wiley & Sons, Ltd. |
| Databáze: | OpenAIRE |
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