H-1-Nmr Studies on Arginine Tripeptides - Evidence for Guanidinium C-Terminal Carboxylate Interactions (Journal article)

Tsikaris, V./ Sakarellos-Daitsiotis, M./ Panoupomonis, E./ Detsikas, E./ Sakarellos, C./ Cung, M. T./ Marraud, M.

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 H-1-NMR spectroscopy. Measurements of the chemical shifts, NOE effects and temperature coefficients showed that the ArgN(epsilon)H and ArgN(eta)H-2 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.
Institution and School/Department of submitter: Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας
Keywords: sequential polypeptides,circular-dichroism,crystal-structures,histone models
URI: https://olympias.lib.uoi.gr/jspui/handle/123456789/8063
ISSN: 1040-5704
Link: <Go to ISI>://A1992HL96700006
Publisher: Eaton Publishing
Appears in Collections:Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά)

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