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| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Troganis, A. | en |
| dc.contributor.author | Stassinopoulou, C. I. | en |
| dc.date.accessioned | 2015-11-24T16:35:09Z | - |
| dc.date.available | 2015-11-24T16:35:09Z | - |
| dc.identifier.issn | 0167-4838 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/7907 | - |
| dc.rights | Default Licence | - |
| dc.subject | concanavalin a | en |
| dc.subject | alpha-d-glycoside | en |
| dc.subject | monosaccharide binding | en |
| dc.subject | nmr, -h-1 | en |
| dc.subject | correlation time | en |
| dc.subject | nuclear magnetic-resonance | en |
| dc.subject | methyl-d-glucopyranoside | en |
| dc.subject | binding-site | en |
| dc.subject | saccharides | en |
| dc.subject | relaxation | en |
| dc.title | Modes of Association of Concanavalin-a with Alpha-D-Glycosides | en |
| heal.type | journalArticle | - |
| heal.type.en | Journal article | en |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.identifier.primary | Doi 10.1016/0167-4838(94)90211-9 | - |
| heal.identifier.secondary | <Go to ISI>://A1994NU75000009 | - |
| heal.language | en | - |
| heal.access | campus | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών και Τεχνολογιών. Τμήμα Βιολογικών Εφαρμογών και Τεχνολογιών | el |
| heal.publicationDate | 1994 | - |
| heal.abstract | Complexes of Con A with alpha-D-glycosides were studied using H-1-NMR, ESR and fluorescence methods. Correlation times, tau(c), for the interaction of the aglycon protons with the manganese ion, present at the S1 site of the protein, were calculated from T-1 measurements at two frequencies. The protons of aromatic aglycons have tau(c) values comparable to the rotational correlation time of the protein molecule, whereas those of non-aromatic aglycons have tau(c)s 10 to 100 times lower. The correlation times were combined with the experimentally acquired paramagnetic contributions to proton relaxation due to the presence of the manganese ion to yield manganese-proton distances. These distances show that aromatic aglycons have additional favorable contacts with the protein which stabilize the lectin-saccharide interaction. The results are compared to the crystal structure of the methyl alpha-D-glycopyranoside complex with Con A and to models earlier proposed for the binding of monosaccharides to Con A. | en |
| heal.journalName | Biochimica Et Biophysica Acta-Protein Structure and Molecular Enzymology | en |
| heal.journalType | peer reviewed | - |
| heal.fullTextAvailability | TRUE | - |
| Appears in Collections: | Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά) | |
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