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 t
Proton nuclear magnetic resonance study of the biologically active peptide analog [Pro2]thymopentin
β Scribed by Guy K. Griffith; Dee-Hua Huang; David G. Nettesheim; George A. Heavner; N. Rama Krishna
- Publisher
- John Wiley and Sons
- Year
- 1989
- Tongue
- English
- Weight
- 177 KB
- Volume
- 27
- Category
- Article
- ISSN
- 0749-1581
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β¦ Synopsis
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 coupling constants and the amide hydrogen exchange rates were measured. The hydrogen exchange rates for Val4 NH and Tyr' NH are more than six times slower than the predicted values for the corresponding solvated peptides. The guanidino N'H proton of the Arg' residue shows a downfield shift with a pK, of 3.5 as the pH is increased. The conformational properties of [Pro'] -thymopentin were compared with those of two other closely related immunoregulatory peptides, thymopentin and [Glu3]TP5 (SP5).
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