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| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Nunes, A. M. P. C. | en |
| dc.contributor.author | Zavitsanos, K. | en |
| dc.contributor.author | Del Conte, R. | en |
| dc.contributor.author | Malandrinos, G. | en |
| dc.contributor.author | Hadjiliadis, N. | en |
| dc.date.accessioned | 2015-11-24T16:40:14Z | - |
| dc.date.available | 2015-11-24T16:40:14Z | - |
| dc.identifier.issn | 1477-9226 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/8250 | - |
| dc.rights | Default Licence | - |
| dc.subject | protein secondary structure | en |
| dc.subject | nucleosome core particle | en |
| dc.subject | pulsed-field gradients | en |
| dc.subject | chemical-shift index | en |
| dc.subject | human protamine hp2 | en |
| dc.subject | nickel-carcinogenesis | en |
| dc.subject | terminal peptide | en |
| dc.subject | coordination properties | en |
| dc.subject | molecular mechanisms | en |
| dc.subject | angstrom resolution | en |
| dc.title | Interaction of histone H2B (fragment 63-93) with Ni(II). An NMR study | en |
| heal.type | journalArticle | - |
| heal.type.en | Journal article | en |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.identifier.primary | Doi 10.1039/B817411c | - |
| heal.identifier.secondary | <Go to ISI>://000263840500005 | - |
| heal.language | en | - |
| heal.access | campus | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας | el |
| heal.publicationDate | 2009 | - |
| heal.abstract | The behaviour of the 31 mer peptide (Ac-NSFVNDIFERIAG(13)EASRL(18)A(19)H(20)YNKRS(25)TITSRE-NH(2)), modelling the histone-fold domain (63 to 93 residues) of H2B, towards Ni(II) was investigated by multidimensional NMR spectroscopy (1D, 2D TOCSY, NOESY and (13)C-HSQC). The coordination involved the imidazole of His20 and three amide nitrogens of His20, Ala19 and Leu18, similar to the one shown by the hexapeptide LAHYNK contained in the 31 mer peptide. The solution structure of the Ni(II) complex with the tridecapeptide comprising histone's H2B 75-87 residues, was elucidated from the NOE cross correlations observed in the 2D-NOESY spectrum. A severe change in the peptide's conformation was observed, passing from a partially helical to a well-defined ordered structure around the metal ion. A remarkable structural feature is the position of the aromatic ring of Tyr21 below the coordination plane. This and the hydrophobic fence created by Leu18 and Ala19, together with the position of Arg17 and Arg24 side chains seem to be relevant to the complex stability. We believe that these structural modi. cations may be physiologically important in the mechanism of nickel induced carcinogenesis. | en |
| heal.journalName | Dalton Transactions | 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 | |
|---|---|---|---|---|
| Malandrinos-2009-Interaction of histone H2B.pdf | 713.63 kB | Adobe PDF | View/Open Request a copy |
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