The solution conformation of the pentapeptide Arg-Pro-Asp-Val-Tyr ( [Pro2]TP5), a biologically active analog of the immunoregulatory peptide thymopentin, Arg-Lys-Asp-Val-Tyr (TP5). was investigated by proton nuclear magnetic resonance spectroscopy. The chemical shift variations with pH, the vicinal
Nuclear magnetic resonance study of the sodium salt of mutalomycin, a structural analog of lonomycin
β Scribed by Weiguo Zhang; Marc J. O. Anteunis; Frans A. M. Borremans
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 2010
- Weight
- 337 KB
- Volume
- 97
- Category
- Article
- ISSN
- 0037-9646
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β¦ Synopsis
The complete assignment of the proton NMR spectrum of the sodium salt of mutalomycin in chloroform was obtained by applying homo-and heteronuclear shift correlation techniques. From the observed chemical shifts and coupling constants the conformation of the title compound is discussed, in relation to its structural analog lonomycin A.
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