The authors state no conflict of interest.
Histidine in continuum electrostatics protonation state calculations†
Article first published online: 30 AUG 2011
Copyright © 2011 Wiley-Liss, Inc.
Proteins: Structure, Function, and Bioinformatics
Special Issue: Protein Electrostatics Calculations: Critical Assessment of Progress and Problems
Volume 79, Issue 12, pages 3410–3419, December 2011
How to Cite
Couch, V. and Stuchebrukhov, A. (2011), Histidine in continuum electrostatics protonation state calculations. Proteins, 79: 3410–3419. doi: 10.1002/prot.23114
- Issue published online: 10 NOV 2011
- Article first published online: 30 AUG 2011
- Accepted manuscript online: 15 JUL 2011 11:14AM EST
- Manuscript Accepted: 8 JUN 2011
- Manuscript Revised: 15 APR 2011
- Manuscript Received: 2 NOV 2010
- NSF. Grant Number: PHY 0646273
- NIH. Grant Number: GM54052
- protein pKa;
- respiratory complex I;
- redox Bohr effect
A modification to the standard continuum electrostatics approach to calculate protein pKas, which allows for the decoupling of histidine tautomers within a two-state model, is presented. Histidine with four intrinsically coupled protonation states cannot be easily incorporated into a two-state formalism, because the interaction between the two protonatable sites of the imidazole ring is not purely electrostatic. The presented treatment, based on a single approximation of the interrelation between histidine's charge states, allows for a natural separation of the two protonatable sites associated with the imidazole ring as well as the inclusion of all protonation states within the calculation. Proteins 2011; © 2011 Wiley-Liss, Inc.