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. 1995 Jan;68(1):5–12. doi: 10.1016/S0006-3495(95)80156-6

Normal modes as refinement parameters for the F-actin model.

M M Tirion 1, D ben-Avraham 1, M Lorenz 1, K C Holmes 1
PMCID: PMC1281655  PMID: 7711267

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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