Site specificity of the (alpha)C--H bond dissociation energy for a naturally occurring beta-hairpin peptide-An ab initio study
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 (alpha)C--H bond dissociation energy of three different glycyl radicals located at different sites o...
| Publié dans: | Journal of computational chemistry. - 1984. - 30(2009), 3 vom: 10. Feb., Seite 407-14 |
|---|---|
| Auteur principal: | |
| Autres auteurs: | , , , , |
| Format: | Article en ligne |
| Langue: | English |
| Publié: |
2009
|
| Accès à la collection: | Journal of computational chemistry |
| Sujets: | Journal Article Research Support, Non-U.S. Gov't Peptides Proteins |
| Résumé: | 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 (alpha)C--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 (alpha)C--H bond strength varied dramatically among these different sites |
|---|---|
| Description: | Date Completed 23.02.2009 Date Revised 29.12.2008 published: Print Citation Status MEDLINE |
| ISSN: | 1096-987X |
| DOI: | 10.1002/jcc.21066 |