Please use this identifier to cite or link to this item:
https://olympias.lib.uoi.gr/jspui/handle/123456789/9203Full metadata record
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Orlewski, P. | en |
| dc.contributor.author | Tsikaris, V. | en |
| dc.contributor.author | Sakarellos-Daitsiotis, M. | en |
| dc.contributor.author | Sakarellos, C. | en |
| dc.contributor.author | Soteriadou, K. P. | en |
| dc.contributor.author | Marraud, M. | en |
| dc.contributor.author | Cung, M. T. | en |
| dc.date.accessioned | 2015-11-24T16:47:33Z | - |
| dc.date.available | 2015-11-24T16:47:33Z | - |
| dc.identifier.issn | 0929-5666 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/9203 | - |
| dc.rights | Default Licence | - |
| dc.subject | leishmania gp63 | en |
| dc.subject | 2d nmr | en |
| dc.subject | molecular dynamics | en |
| dc.subject | dmso solvent box | en |
| dc.subject | arginine ionic bridge | en |
| dc.subject | beta i-turn | en |
| dc.subject | dimethyl-sulfoxide | en |
| dc.subject | recognition site | en |
| dc.subject | cell-adhesion | en |
| dc.subject | rgd | en |
| dc.subject | peptides | en |
| dc.subject | grgdsp | en |
| dc.title | Solution structure of an SRYD-containing sequence (250-257) of the fibronectin-like Leishmania gp63 protein by restrained molecular dynamics | en |
| heal.type | journalArticle | - |
| heal.type.en | Journal article | en |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.identifier.secondary | <Go to ISI>://A1996WA48200007 | - |
| heal.identifier.secondary | http://www.springerlink.com/content/h5x231333042l588/fulltext.pdf | - |
| heal.language | en | - |
| heal.access | campus | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας | el |
| heal.publicationDate | 1996 | - |
| heal.abstract | The IASRYDQL synthetic octapeptide (250-257) of the Leishmania major surface glycoprotein gp63 efficiently inhibits parasite attachment to the macrophage receptors in in vitro experiments, and the SRYD-containing tetrapeptide mimics antigenically and functionally the RGDS sequence of fibronectin. The conformational properties of the octapeptide were investigated in dimethylsulfoxide (DMSO) with the combined use of NMR data (vicinal coupling constants, nuclear Overhauser effects (NOEs) and temperature coefficient values), molecular modeling by energy minimization and molecular dynamics. The structure is characterized by the high occurrence, exceeding 95%, of the Arg-Asp side-chain-side-chain ionic interaction, which plays a key role in the backbone folding through a distorted type-I beta-turn involving the Gln(256)-NH to Arg(253)-CO hydrogen bond. | en |
| heal.publisher | Kluwer Academic Publishers | en |
| heal.journalName | Letters in Peptide Science | en |
| heal.journalType | peer reviewed | - |
| heal.fullTextAvailability | TRUE | - |
| Appears in Collections: | Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά). ΧΗΜ | |
Files in This Item:
| File | Description | Size | Format | |
|---|---|---|---|---|
| Orlewski-1996-Solution structure o.pdf | 568.62 kB | Adobe PDF | View/Open Request a copy |
This item is licensed under a Creative Commons License
