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Use of natural-abundance 15N-nmr spectroscopy to investigate the secondary structure of peptides: Gramicidin S

✍ Scribed by Geoffrey E. Hawkes; Edward W. Randall; William E. Hull; Odile Convert

Publisher
Wiley (John Wiley & Sons)
Year
1980
Tongue
English
Weight
615 KB
Volume
19
Category
Article
ISSN
0006-3525

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✦ Synopsis

Abstract

The natural‐abundance ^15^N‐nuclear magnetic resonance (nmr) spectrum of the cyclic decapeptide gramicidin S has been measured and assigned in the solvents dimethyl sulfoxide, methanol, and 2,2,2‐trifluoroethanol. Three methods have been investigated to distinguish between peptide groups which are exposed to or shielded from the solvent. The solvent dependence of the ^15^N chemical shift is correlated with the two types of peptide group in gramicidin Sthose with the carbonyl group exposed or shielded from the solvent. The second method monitors the lability of the N__H__ proton (via the collapse of the reduced ^15^N‐^1^H coupling) in the presence of added base used to promote intermolecular exchange—peptide protons shielded from the solvent exchange more slowly. The third method looks at the temperature dependence of the ^15^N chemical shifts in dimethyl sulfoxide. Here the data are not so distinctive as to allow the differentiation between solvent‐exposed or shielded NH bonds at all peptide groups.

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