New force field parameters for metalloproteins I : Divalent copper ion centers including three histidine residues and an oxygen-ligated amino acid residue

Copyright © 2014 Wiley Periodicals, Inc.

Bibliographische Detailangaben
Veröffentlicht in:Journal of computational chemistry. - 1984. - 35(2014), 17 vom: 30. Juni, Seite 1278-89
1. Verfasser: Wise, Olivia (VerfasserIn)
Weitere Verfasser: Coskuner, Orkid
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2014
Zugriff auf das übergeordnete Werk:Journal of computational chemistry
Schlagworte:Journal Article Research Support, Non-U.S. Gov't first principles force field parameters metalloproteins molecular dynamics simulations Metalloproteins Aspartic Acid 30KYC7MIAI Glutamic Acid mehr... 3KX376GY7L Tyrosine 42HK56048U Histidine 4QD397987E Copper 789U1901C5
Beschreibung
Zusammenfassung:Copyright © 2014 Wiley Periodicals, Inc.
Transition metal ion complexation with proteins is ubiquitous across such diverse fields as neurodegenerative and cardiovascular diseases and cancer. In this study, the structures of divalent copper ion centers including three histidine and one oxygen-ligated amino acid residues and the relative binding affinities of the oxygen-ligated amino acid residues with these metal ion centers, which are debated in the literature, are presented. Furthermore, new force field parameters, which are currently lacking for the full-length metal-ligand moieties, are developed for metalloproteins that have these centers. These new force field parameters enable investigations of metalloproteins possessing these binding sites using molecular simulations. In addition, the impact of using the atom equivalence and inequivalence atomic partial charge calculation procedures on the simulated structures of these metallopeptides, including hydration properties, is described
Beschreibung:Date Completed 20.04.2015
Date Revised 23.05.2014
published: Print-Electronic
Citation Status MEDLINE
ISSN:1096-987X
DOI:10.1002/jcc.23622