help button home button Biophys. J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Ravichandran, S.
Right arrow Articles by Talbot, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ravichandran, S.
Right arrow Articles by Talbot, J.

Biophys J, January 2000, p. 110-120, Vol. 78, No. 1

Mobility of Adsorbed Proteins: A Brownian Dynamics Study

S. Ravichandran and J. Talbot

Department of Chemistry and Biochemistry, Duquesne University, Pittsburgh, Pennsylvania 15282 USA

We simulate the adsorption of lysozyme on a solid surface, using Brownian dynamics simulations. A protein molecule is represented as a uniformly charged sphere and interacts with other molecules through screened Coulombic and double-layer forces. The simulation starts from an empty surface and attempts are made to introduce additional proteins at a fixed time interval that is inversely proportional to the bulk protein concentration. We examine the effect of ionic strength and bulk protein concentration on the adsorption kinetics over a range of surface coverages. The structure of the adsorbed layer is examined through snapshots of the configurations and quantitatively with the radial distribution function. We extract the surface diffusion coefficient from the mean square displacement. At high ionic strengths the Coulombic interaction is effectively shielded, leading to increased surface coverage. This effect is quantified with an effective particle radius. Clustering of the adsorbed molecules is promoted by high ionic strength and low bulk concentrations. We find that lateral protein mobility decreases with increasing surface coverage. The observed trends are consistent with previous theoretical and experimental studies.

Biophys J, January 2000, p. 110-120, Vol. 78, No. 1
© 2000 by the Biophysical Society   0006-3495/00/01/110/11  $2.00



This article has been cited by other articles:


Home page
Biophys. JHome page
C. Czeslik, C. Royer, T. Hazlett, and W. Mantulin
Reorientational Dynamics of Enzymes Adsorbed on Quartz: A Temperature-Dependent Time-Resolved TIRF Anisotropy Study
Biophys. J., April 1, 2003; 84(4): 2533 - 2541.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
C. Calonder, Y. Tie, and P. R. Van Tassel
History dependence of protein adsorption kinetics
PNAS, September 4, 2001; (2001) 181337298.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
J. Satulovsky, M. A. Carignano, and I. Szleifer
Kinetic and thermodynamic control of protein adsorption
PNAS, July 19, 2000; (2000) 150236197.
[Abstract] [Full Text]


Home page
Proc. Natl. Acad. Sci. USAHome page
J. Satulovsky, M. A. Carignano, and I. Szleifer
Kinetic and thermodynamic control of protein adsorption
PNAS, August 1, 2000; 97(16): 9037 - 9041.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
C. Calonder, Y. Tie, and P. R. Van Tassel
History dependence of protein adsorption kinetics
PNAS, September 11, 2001; 98(19): 10664 - 10669.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2000 by the Biophysical Society.