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Molecular Dynamics of a Protein Surface: Ion-Residues Interactions
Laser Laboratory for Fast Reactions in Biology, Department of Biochemistry, The George S. Wise Faculty for Life Sciences, Tel Aviv University, Tel Aviv, Israel.ORCID iD: 0000-0001-8696-3104
2005 (English)In: Biophysical Journal, ISSN 0006-3495, E-ISSN 1542-0086, Vol. 89, no 2, 768-781 p.Article in journal (Refereed) Published
Abstract [en]

Time-resolved measurements indicated that protons could propagate on the surface of a protein or a membrane by a special mechanism that enhanced the shuttle of the proton toward a specific site. It was proposed that a suitable location of residues on the surface contributes to the proton shuttling function. In this study, this notion was further investigated by the use of molecular dynamics simulations, where Na+ and Clare the ions under study, thus avoiding the necessity for quantum mechanical calculations. Molecular dynamics simulations were carried out using as a model a few Na+ and Cl ions enclosed in a fully hydrated simulation box with a small globular protein (the S6 of the bacterial ribosome). Three independent 10-ns-long simulations indicated that the ions and the protein's surface were in equilibrium, with rapid passage of the ions between the protein's surface and the bulk. However, it was noted that close to some domains the ions extended their duration near the surface, thus suggesting that the local electrostatic potential hindered their diffusion to the bulk. During the time frame in which the ions were detained next to the surface, they could rapidly shuttle between various attractor sites located under the electrostatic umbrella. Statistical analysis of the molecular dynamics and electrostatic potential/entropy consideration indicated that the detainment state is an energetic compromise between attractive forces and entropy of dilution. The similarity between the motion of free ions next to a protein and the proton transfer on the protein's surface are discussed.

Place, publisher, year, edition, pages
2005. Vol. 89, no 2, 768-781 p.
National Category
Biophysics
Research subject
Natural Science
Identifiers
URN: urn:nbn:se:lnu:diva-14237DOI: 10.1529/biophysj.105.058917OAI: oai:DiVA.org:lnu-14237DiVA: diva2:445503
Available from: 2011-10-04 Created: 2011-09-16 Last updated: 2015-05-26Bibliographically approved

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CiteExportLink to record
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