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Normal modes as refinement parameters for the f-actin model

MPS-Authors
/persons/resource/persons95655

Tirion,  Monique
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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Lorenz,  Michael
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;
Department of Biomedical Optics, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons93463

Holmes,  Kenneth C.
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

External Resource

http://www.sciencedirect.com/science/article/pii/S0006349595801566/pdf?md5=db6f3daa2a5f68dffa1ac0a77b7de6d0&pid=1-s2.0-S0006349595801566-main.pdf
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http://dx.doi.org/10.1016/S0006-3495(95)80156-6
(Any fulltext)

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Citation

Tirion, M., Ben-Avraham, D., Lorenz, M., & Holmes, K. C. (1995). Normal modes as refinement parameters for the f-actin model. Biophysical Journal, 68(1), 5-12. doi:10.1016/S0006-3495(95)80156-6.


Cite as: https://hdl.handle.net/11858/00-001M-0000-002B-5008-4
Abstract
The slow normal modes of G-actin were used as structural parameters to refine the F-actin model against 8-A resolution x-ray fiber diffraction data. The slowest frequency normal modes of G-actin pertain to collective rearrangements of domains, motions that are characterized by correlation lengths on the order of the resolution of the fiber diffraction data. Using a small number of normal mode degrees of freedom (< or = 12) improved the fit to the data significantly. The refined model of F-actin shows that the nucleotide binding cleft has narrowed and that the DNase I binding loop has twisted to a lower radius, consistent with other refinement techniques and electron microscopy data. The methodology of a normal mode refinement is described, and the results, as applied to actin, are detailed.