Premium
Site specificity of the α CH bond dissociation energy for a naturally occurring β‐hairpin peptide—An ab initio study
Author(s) -
Cheng WanChun,
Jang Soonmin,
Wu ChenChang,
Lin RenJie,
Lu HsiuFeng,
Li FengYin
Publication year - 2009
Publication title -
journal of computational chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.907
H-Index - 188
eISSN - 1096-987X
pISSN - 0192-8651
DOI - 10.1002/jcc.21066
Subject(s) - chemistry , peptide , radical , ab initio , peptide bond , crystallography , bond dissociation energy , dissociation (chemistry) , ab initio quantum chemistry methods , stereochemistry , computational chemistry , molecule , organic chemistry , biochemistry
A naturally occurring β‐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 α CH bond dissociation energy of three different glycyl radicals located at different sites on the β‐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 α‐H abstracted β‐hairpin peptide remained almost unchanged with the exception of the local conformation of the attacked residue. However, the α CH bond strength varied dramatically among these different sites. © 2008 Wiley Periodicals, Inc. J Comput Chem, 2009