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| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Tsikaris, V. | en |
| dc.contributor.author | Sakarellos-Daitsiotis, M. | en |
| dc.contributor.author | Panoupomonis, E. | en |
| dc.contributor.author | Detsikas, E. | en |
| dc.contributor.author | Sakarellos, C. | en |
| dc.contributor.author | Cung, M. T. | en |
| dc.contributor.author | Marraud, M. | en |
| dc.date.accessioned | 2015-11-24T16:38:35Z | - |
| dc.date.available | 2015-11-24T16:38:35Z | - |
| dc.identifier.issn | 1040-5704 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/8063 | - |
| dc.rights | Default Licence | - |
| dc.subject | sequential polypeptides | en |
| dc.subject | circular-dichroism | en |
| dc.subject | crystal-structures | en |
| dc.subject | histone models | en |
| dc.title | H-1-Nmr Studies on Arginine Tripeptides - Evidence for Guanidinium C-Terminal Carboxylate Interactions | en |
| heal.type | journalArticle | - |
| heal.type.en | Journal article | en |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.identifier.secondary | <Go to ISI>://A1992HL96700006 | - |
| heal.language | en | - |
| heal.access | campus | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας | el |
| heal.publicationDate | 1992 | - |
| heal.abstract | 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. | en |
| heal.publisher | Eaton Publishing | en |
| heal.journalName | Peptide Research | en |
| heal.journalType | peer reviewed | - |
| heal.fullTextAvailability | TRUE | - |
| Appears in Collections: | Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά). ΧΗΜ | |
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