Dielectric properties of proteins from simulation: The effects of solvent, ligands, pH, and temperature

Pitera, Jed W., Falta, Michael, & van Gunsteren, Wilfred F. (2001) Dielectric properties of proteins from simulation: The effects of solvent, ligands, pH, and temperature. Biophysical Journal, 80(6), pp. 2546-2555.


We have used a standard Fröhlich-Kirkwood dipole moment fluctuation model to calculate the static dielectric permittivity, epsilon(0), for four different proteins, each of which was simulated under at least two different conditions of pH, temperature, solvation, or ligand binding. For the range of proteins and conditions studied, we calculate values for epsilon(0) between 15 and 40. Our results show, in agreement with prior work, that the behavior of charged residues is the primary determinant of the effective permittivity. Furthermore, only environmental changes that alter the properties of charged residues exert a significant effect on epsilon. In contrast, buried water molecules or ligands have little or no effect on protein dielectric properties.

Impact and interest:

108 citations in Scopus
97 citations in Web of Science®
Search Google Scholar™

Citation counts are sourced monthly from Scopus and Web of Science® citation databases.

These databases contain citations from different subsets of available publications and different time periods and thus the citation count from each is usually different. Some works are not in either database and no count is displayed. Scopus includes citations from articles published in 1996 onwards, and Web of Science® generally from 1980 onwards.

Citations counts from the Google Scholar™ indexing service can be viewed at the linked Google Scholar™ search.

Full-text downloads:

305 since deposited on 11 Jul 2007
9 in the past twelve months

Full-text downloads displays the total number of times this work’s files (e.g., a PDF) have been downloaded from QUT ePrints as well as the number of downloads in the previous 365 days. The count includes downloads for all files if a work has more than one.

ID Code: 8556
Item Type: Journal Article
Refereed: Yes
Additional URLs:
ISSN: 0006-3495
Subjects: Australian and New Zealand Standard Research Classification > PHYSICAL SCIENCES (020000) > OTHER PHYSICAL SCIENCES (029900) > Biological Physics (029901)
Divisions: Current > QUT Faculties and Divisions > QUT Business School
Copyright Owner: Copyright 2001 Biophysical Society
Copyright Statement: Reproduced in accordance with the copyright policy of the publisher.
Deposited On: 11 Jul 2007 00:00
Last Modified: 05 Jan 2011 13:32

Export: EndNote | Dublin Core | BibTeX

Repository Staff Only: item control page