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標題: Site Specificity of the C-alpha-H Bond Dissociation Energy for a Naturally Occurring beta-Hairpin Peptide-An Ab Initio Study
作者: Cheng, W.C.
Jang, S.M.
Wu, C.C.
Lin, R.J.
Lu, H.F.
Li, F.Y.
關鍵字: beta-hairpin;alpha-C-center radical;naturally occurring;bond;dissociation energy;quantum-mechanical approach;hydrogen abstraction reaction;molecular-orbital method;amino-acid-residues;protein oxidation;methionine oxidation;alzheimers-disease;secondary structure;rate;coefficients;aqueous-solution
Project: Journal of Computational Chemistry
期刊/報告no:: Journal of Computational Chemistry, Volume 30, Issue 3, Page(s) 407-414.
A naturally occurring beta-hairpin peptide (PDB ID 1UAO) was used as a model to study the backbone oxidation of a protein with ab initio calculation at the B3LYB/6-31G(d) without any constraints. The C-alpha-H bond dissociation energy of three different glycyl radicals located at different sites on the beta-hairpin peptide was calculated to evaluate the site specificity of backbone oxidation. The molecular and electronic structures of these glycyl radicals were analyzed to rationalize this site specificity. The overall molecular structure of the alpha-H abstracted beta-hairpin peptide remained almost unchanged with the exception of the local conformation of the attacked residue. However. the C-alpha-H bond strength varied dramatically among these different sites. (C) 2008 Wiley Periodicals. Inc.
ISSN: 0192-8651
DOI: 10.1002/jcc.21066
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