Please use this identifier to cite or link to this item:
https://olympias.lib.uoi.gr/jspui/handle/123456789/8597Full metadata record
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Tsikaris, V. | en |
| dc.contributor.author | Cung, M. T. | en |
| dc.contributor.author | Sakarellos, C. | en |
| dc.contributor.author | Tzinia, A. K. | en |
| dc.contributor.author | Soterladou, K. P. | en |
| dc.contributor.author | Sakarellos-Daitsiotis, M. | en |
| dc.date.accessioned | 2015-11-24T16:42:47Z | - |
| dc.date.available | 2015-11-24T16:42:47Z | - |
| dc.identifier.issn | 0300-9580 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/8597 | - |
| dc.rights | Default Licence | - |
| dc.subject | cell-adhesion | en |
| dc.subject | spectroscopy | en |
| dc.subject | peptides | en |
| dc.subject | region | en |
| dc.subject | rgd | en |
| dc.title | Nmr-Study on a Sryd-Containing Fibronectin-Like Sequence-(250-257) of Leishmania-Gp63 - Contribution of Residual Water in the Dimethyl-Sulfoxide Solution Structure | en |
| heal.type | journalArticle | - |
| heal.type.en | Journal article | en |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.identifier.primary | 10.1039/P29940000821 | - |
| heal.identifier.secondary | <Go to ISI>://A1994NF45100028 | - |
| heal.language | en | - |
| heal.access | campus | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας | el |
| heal.publicationDate | 1994 | - |
| heal.abstract | The conformational characteristics of the I(250)ASRYDQL(257) synthetic octapeptide, which incorporates the SRYD adhesion site (252-255) of Leishmania gp63, have been investigated at pH 2 and 5, by means of 1D and 2D H-1 NMR spectroscopy (temperature coefficient values, chemical shifts, vicinal coupling constants and NOE effects). It was found that elimination of residual water from the dimethyl sulfoxide (DMSO) solution at pH 2 provides exchange peaks in the ROESY and HOHAHA spectra similar to those obtained for the DMSO peptide solution at pH 5. This common structure is stabilized (i) by the formation of a type I beta-turn involving the QNH --> RCO interaction and (ii) by a possible interaction between the guanidinium and the D-beta-carboxylate groups. After treatment with molecular sieves, the remaining residual water is redistributed between the peptide functional groups and participates in the rigidification of the new conformational state. | en |
| heal.publisher | Royal Society of Chemistry | en |
| heal.journalName | Journal of the Chemical Society-Perkin Transactions 2 | en |
| heal.journalType | peer reviewed | - |
| heal.fullTextAvailability | TRUE | - |
| Appears in Collections: | Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά). ΧΗΜ | |
Files in This Item:
There are no files associated with this item.
This item is licensed under a Creative Commons License
