Journal article
Computer simulations of actin polymerization can explain the barbed-pointed end asymmetry
Journal of molecular biology, Vol.294(5), pp.1181-1189
1999
DOI: 10.1006/jmbi.1999.3332
PMID: 10600376
Abstract
Computer simulations of actin polymerization were performed to investigate the role of electrostatic interactions in determining polymerization rates. Atomically detailed models of actin monomers and filaments were used in conjunction with a Brownian dynamics method. The simulations were able to reproduce the measured barbed end association rates over a range of ionic strengths and predicted a slower growing pointed end, in agreement with experiment. Similar simulations neglecting electrostatic interactions indicate that configurational and entropic factors may actually favor polymerization at the pointed end, but electrostatic interactions remove this trend. This result would indicate that polymerization at the pointed end is not only limited by diffusion, but faces electrostatic forces that oppose binding. The binding of the actin depolymerizing factor (ADF) and G-actin complex to the end of a filament was also simulated. In this case, electrostatic steering effects lead to an increase in the simulated association rate. Together, the results indicate that simulations provide a realistic description of both polymerization and the binding of more complex structures to actin filaments.
Details
- Title: Subtitle
- Computer simulations of actin polymerization can explain the barbed-pointed end asymmetry
- Creators
- David Sept - Department of Chemistry and Biochemistry University of California at San Diego, La Jolla, CA 92093-0365, USAAdrian H Elcock - Department of Chemistry and Biochemistry University of California at San Diego, La Jolla, CA 92093-0365, USAJ.Andrew McCammon - Department of Chemistry and Biochemistry University of California at San Diego, La Jolla, CA 92093-0365, USA
- Resource Type
- Journal article
- Publication Details
- Journal of molecular biology, Vol.294(5), pp.1181-1189
- Publisher
- Elsevier Ltd
- DOI
- 10.1006/jmbi.1999.3332
- PMID
- 10600376
- ISSN
- 0022-2836
- eISSN
- 1089-8638
- Language
- English
- Date published
- 1999
- Academic Unit
- Physics and Astronomy; Biochemistry and Molecular Biology
- Record Identifier
- 9984025288302771
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