1H-NMR studies on arginine tripeptides: evidence for guanidinium-C-terminal carboxylate interactions

 
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1992 (EN)
1H-NMR studies on arginine tripeptides: evidence for guanidinium-C-terminal carboxylate interactions (EN)

V.Tsikaris (EN)

Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας (EL)
V.Tsikaris (EN)

Guanidinium-C-terminal carboxylate interactions are involved in the establishment of the secondary structure of various biologically active peptide sequences. The conformational properties of a series of arginine-containing tripeptides, L-Arg-X-Gly (X = L-Ala, Val, Leu), in DMSO solutions at physiological pH, have been studied by means of 1D and 2D 1H-NMR spectroscopy. Measurements of the chemical shifts, NOE effects and temperature coefficients showed that the ArgN epsilon H and ArgN eta H2 groups form two hydrogen bonds with the C-terminal carboxylate moiety, whereas the ArgN alpha-terminal nitrogen is in the amino state. Our results point out the significant contribution of the C-terminal carboxylate group, at physiological pH, in the stabilization of the Arg side-chain structure in peptides simultaneously containing arginine residues and carboxy terminal sequences. (EN)

Πανεπιστήμιο Ιωαννίνων (EL)
University of Ioannina (EN)

Peptide Research (EN)

1992




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