@article {431,
	title = {Allostery of Actin Filaments: Molecular Dynamics Simulations and Coarse-grained Analysis},
	journal = {Proc Natl Acad Sci U S A},
	volume = {102},
	number = {37},
	year = {2005},
	note = {Chu, Jhih-Wei Voth, Gregory A 1 S10RR17214-01/RR/NCRR NIH HHS/United States Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov{\textquoteright}t Research Support, U.S. Gov{\textquoteright}t, Non-P.H.S. Research Support, U.S. Gov{\textquoteright}t, P.H.S. United States Proceedings of the National Academy of Sciences of the United States of America Proc Natl Acad Sci U S A. 2005 Sep 13;102(37):13111-6. Epub 2005 Aug 31.},
	pages = {13111-6},
	abstract = {<p>The structural and mechanical properties of monomeric actin (G-actin), the trimer nucleus, and actin filaments (F-actins) are determined as a function of the conformation of the DNase I-binding loop (DB loop) by using all-atom molecular dynamics simulations and coarse-grained (CG) analysis. Recent x-ray structures of ADP-bound G-actin (G-ADP) by Otterbein et al. [Otterbein, L. R., Graceffa, P. \&amp; Dominguez, R. (2001) Science 293, 708-711] and ATP-bound G-actin (G-ATP) by Graceffa and Dominguez [Graceffa, P. \&amp; Dominguez, R. (2003) J. Biol. Chem. 278, 34172-34180] indicate that the DB loop of actin does not have a well defined secondary structure in the ATP state but folds into an alpha-helix in the ADP state. MD simulations and CG analysis indicate that such a helical DB loop significantly weakens the intermonomer interactions of actin assemblies and thus leads to a wider, shorter, and more disordered filament. The computed persistence lengths of F-actin composed of G-ATP (16 microm) and of G-ADP (8.5 microm) agree well with the experimental values for the two states. Therefore, the loop-to-helix transition of the DB loop may be one of the factors that lead to the changes in structural and mechanical properties of F-actin after ATP hydrolysis. This result may provide a direct connection between the conformational changes of an actin monomer and the structural and mechanical properties of the cytoskeleton. The information provided by MD simulations also helps to understand the possible origin of the special features of actin dynamics.</p>},
	keywords = {Actin Cytoskeleton/*chemistry Actins/chemistry Adenosine Diphosphate/analogs \& derivatives/chemistry Adenosine Triphosphate/analogs \& derivatives/chemistry/metabolism *Allosteric Site Animals Binding Sites Computer Simulation Deoxyribonuclease I Humans *M, Molecular Motion Protein Binding Protein Structure, Secondary},
	doi = {10.1073/pnas.0503732102},
	author = {Chu, J. W. and G. A. Voth}
}
