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| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Takis, P. G. | en |
| dc.contributor.author | Melissas, V. S. | en |
| dc.contributor.author | Troganis, A. N. | en |
| dc.date.accessioned | 2015-11-24T16:52:19Z | - |
| dc.date.available | 2015-11-24T16:52:19Z | - |
| dc.identifier.issn | 1144-0546 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/9865 | - |
| dc.rights | Default Licence | - |
| dc.subject | relative hydration numbers | en |
| dc.subject | spin-lattice relaxation | en |
| dc.subject | gas-phase | en |
| dc.subject | nmr relaxation | en |
| dc.subject | intramolecular motion | en |
| dc.subject | zwitterionic forms | en |
| dc.subject | chemical-exchange | en |
| dc.subject | aqueous-solution | en |
| dc.subject | aspartic-acid | en |
| dc.subject | l-alanine | en |
| dc.title | A "hidden" role of amino and imino groups is unveiled during the micro-solvation study of three biomolecule groups in water | en |
| heal.type | journalArticle | - |
| heal.type.en | Journal article | en |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.identifier.primary | Doi 10.1039/C2nj40390k | - |
| heal.identifier.secondary | <Go to ISI>://000307451400025 | - |
| heal.identifier.secondary | http://pubs.rsc.org/en/Content/ArticleLanding/2012/NJ/c2nj40390k | - |
| heal.language | en | - |
| heal.access | campus | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας | el |
| heal.publicationDate | 2012 | - |
| heal.abstract | The C-13 longitudinal relaxation times (T-1) of three biomolecule groups of major significance to proteins and cells - protein amino acids (AAs), acetyl-amino acids (Ac-AAs) and betaines - and the N-14 linewidths (Delta nu(1/2)) of Ac-AAs and betaines were measured in aqueous solutions at acidic and neutral pH, by NMR spectroscopy, to estimate the effect of the molecular weight (M-w) on C-13 longitudinal relaxation times and N-14 linewidths, respectively. C-13 relaxation times indicate that AAs and Ac-AAs strongly interact with the same number of water molecules at acidic and neutral pH, respectively, whereas both C-13 and N-14 results indicate that their Mw values at acidic pH (protonated, positively charged AAs and zero-charged Ac-AAs) increase relatively to those at pH 6.0 (zwitterionic AAs and negatively charged Ac-AAs) that translates into their extra hydration with an excess of one water molecule. Both C-13 and N-14 relaxation times revealed that betaines retain their hydration grade in both their ionization states at two pH values, while exhibiting their hydration differences from AAs and Ac-AAs and pointing out the "controlling" role of the amino and imino groups in the extra hydration of protonated AAs and Ac-AAs, enlightening the so far unknown significant role of the N-terminus and the -NH near the C-terminus in peptide solvation. Moreover, DFT calculations of the interacting water molecules through hydrogen bonds with Ala, Ac-Ala and Ala betaine molecules in their protonated and neutral pH forms are in absolute agreement with NMR results. Finally, a fully promising method arises with a view on hydration-solvation studies of oligopeptides and other bio-organic molecules by C-13 relaxation. | en |
| heal.publisher | Springer Verlag (Germany) | en |
| heal.journalName | New Journal of Chemistry | en |
| heal.journalType | peer reviewed | - |
| heal.fullTextAvailability | TRUE | - |
| Appears in Collections: | Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά). ΧΗΜ | |
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