Coordination of Cu(2+) and Ni(2+) with the histone model peptide of H2B N-terminal tail (1-31 residues): A spectroscopic study
| dc.contributor.author | Nunes, A. M. | en |
| dc.contributor.author | Zavitsanos, K. | en |
| dc.contributor.author | Malandrinos, G. | en |
| dc.contributor.author | Hadjiliadis, N. | en |
| dc.date.accessioned | 2015-11-24T16:54:53Z | |
| dc.date.available | 2015-11-24T16:54:53Z | |
| dc.identifier.issn | 1477-9226 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/10214 | |
| dc.rights | Default Licence | - |
| dc.subject | protein secondary structure | en |
| dc.subject | nuclear magnetic-resonance | en |
| dc.subject | pulsed-field gradients | en |
| dc.subject | metal-binding sequence | en |
| dc.subject | chemical-shift index | en |
| dc.subject | nmr-spectroscopy | en |
| dc.subject | nickel(ii) complexes | en |
| dc.subject | aqueous-solution | en |
| dc.subject | copper(ii) complexes | en |
| dc.subject | circular-dichroism | en |
| dc.title | Coordination of Cu(2+) and Ni(2+) with the histone model peptide of H2B N-terminal tail (1-31 residues): A spectroscopic study | en |
| heal.abstract | The interaction of Cu(2+) and Ni(2+) with the N-terminal tail of histone H2B, the 31 amino acid peptide H2B(1-31) (Ac-PEPAKSAPAPKKG(13)SKKAVTKAQKKD(25)GKKRKR-NH(2)), studied by various spectroscopic techniques (UV/Vis, CD, EPR and NMR) are described. The results showed the formation of Cu(2+)-H2B(1-31) complexes above pH 7.3 most probably through the beta-carboxylate group of D25. With the increase of the pH, a mixture of 3 N and 4 N species presenting {2N(-), CO, epsilon NH(2)} and {2N(-), OH(2), epsilon NH(2)}{epsilon NH(2)} coordination modes, respectively is formed, while at highly basic solutions the binding of an additional amide donor is suggested. NMR spectroscopy supported by CD spectroscopy indicated that Ni(2+) coordination takes place most likely through Q22-K23-K24-D25 peptide fragment. Direct coordination to Ni(2+), in a {4N(-)} coordination mode, with a severe conformation change in all residues from G13 to G26 was observed. Cu(2+) and Ni(2+) binding to the N-terminal tail of H2B causes a severe conformational change that might interfere with histone post-translational modi. cations, possibly leading to epigenetic changes. | en |
| heal.access | campus | - |
| heal.fullTextAvailability | TRUE | - |
| heal.identifier.primary | Doi 10.1039/B927157k | - |
| heal.identifier.secondary | <Go to ISI>://000277031800016 | - |
| heal.identifier.secondary | http://pubs.rsc.org/en/content/articlepdf/2010/dt/b927157k | - |
| heal.journalName | Dalton Transactions | en |
| heal.journalType | peer reviewed | - |
| heal.language | en | - |
| heal.publicationDate | 2010 | - |
| heal.publisher | Royal Society of Chemistry | en |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας | el |
| heal.type | journalArticle | - |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.type.en | Journal article | en |
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