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Biophys. J. BioFAST: First Published March 7, 2008. doi:10.1529/biophysj.107.125302
© 2008 by the Biophysical Society.


A more recent version of this article appeared on June 15, 2008.
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PROTEINS

Differences in internal dynamics of actin under different structural states detected by neutron scattering

Satoru Fujiwara 1*, Marie Plazanet 2, Fumiko Matsumoto 1 and Toshiro Oda 3

1 Japan Atomic Energy Agency
2 Univ. di Firenze
3 RIKEN Harima Institute

* To whom correspondence should be addressed. E-mail: fujiwara.satoru{at}jaea.go.jp.

Submitted on November 6, 2007
Revised on December 9, 2007
Accepted on 8 February 2008


   Abstract
F-actin, a helical polymer formed by polymerization of the monomers (G-actin), plays crucial roles in various aspects of cell motility. Flexibility of F-actin has been suggested to be important for such a variety of functions. Understanding the flexibility of F-actin requires characterization of a hierarchy of dynamical properties, from internal dynamics of the actin monomers through domain motions within the monomers and relative motions between the monomers within F-actin to large-scale motions of F-actin as a whole. Here, as a first step towards this ultimate purpose, we carried out elastic incoherent neutron scattering experiments on powders of F-actin and G-actin hydrated with D2O and characterized the internal dynamics of F-actin and G-actin. Well established techniques and analysis enabled the extraction of mean square displacements and their temperature dependence in F-actin and in G-actin. An effective force constant analysis with a model consisting of three energy states showed that two dynamical transitions occur at about 150K and about 245K, the former of which corresponds to the onset of anharmonic motions and the latter of which couples with the transition of hydration water. It is shown that behavior of the mean square displacements is different between "softer" than F-actin. The differences in the internal dynamics are detected for the first time between the different structural states (the monomeric state and the polymerized state) here. The different behavior observed is ascribed to the differences in dynamical heterogeneity between F-actin and G-actin. In confrontation with structural data, the assignment of the differences observed in the two samples to dynamics of specific loop regions involved in the polymerization of G-actin into F-actin is proposed.

Key Words: dynamical transition, elastic incoherent neutron scattering, flexibility of actin, force constant analysis, mean square displacement







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Copyright © 2008 by the Biophysical Society.