Gerlei, Klára Z. and Jensen, Svend J. Knak and Élő, Lilla and Fiser, Béla and Owen, Michael C. and Jákli, Imre and Csizmadia, G. Imre and Perczel, András and Viskolcz, Béla (2014) Impairment of a model peptide by oxidative stress: Thermodynamic stabilities of asparagine diamide C(alpha)-radical foldamers. CHEMICAL PHYSICS LETTERS, 593. pp. 104-108. ISSN 0009-2614
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Abstract
Electron structure calculations on N-acetyl asparagine N-methylamide were performed to identify the global minimum from which radicals were formed after H-abstraction by the OH radical. It was found that the radical generated by breaking the C–H bond of the alpha-carbon was thermodynamically the most stable one in the gas- and aqueous phases. The extended ((beta)L and (beta)D) backbone conformations are the most stable, but syn–syn or inverse gamma-turn ((gamma)L) and gamma-turn ((gamma)D) have substantial stability too. The highest energy conformers are the degenerate eL and eD foldamers. Clearly, the most stable beta foldamer is the most likely intermediate for racemization.
| Item Type: | Article |
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| Additional Information: | This accepted author manuscript is copyrighted and published by Elsevier. It is posted here by agreement between Elsevier and MTA. The definitive version of the text was subsequently published in CHEMICAL PHYSICS LETTERS 593, 104. Available under license CC-BY-NC-ND. |
| Subjects: | Q Science / természettudomány > QD Chemistry / kémia |
| Depositing User: | Dóra K. Menyhárd |
| Date Deposited: | 13 Feb 2015 19:09 |
| Last Modified: | 03 Apr 2023 08:25 |
| URI: | http://real.mtak.hu/id/eprint/21782 |
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