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  An atomic model of the unregulated thin filament obtained by x-ray diffraction on orientated actin-tropomyosin gels

Holmes, K. C. (1995). An atomic model of the unregulated thin filament obtained by x-ray diffraction on orientated actin-tropomyosin gels. Journal of Molecular Biology (London), 246(1), 108-119. doi:10.1006/jmbi.1994.0070.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-002B-4C6E-1 Version Permalink: https://hdl.handle.net/11858/00-001M-0000-002B-4C6F-0
Genre: Journal Article
Alternative Title : An atomic model of the unregulated thin filament obtained by x-ray diffraction on orientated actin-tropomyosin gels

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http://www.sciencedirect.com/science/article/pii/S0022283684700702/pdf?md5=ba339d10ef03084d308de92f855b404c&pid=1-s2.0-S0022283684700702-main.pdf (Any fulltext)
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 Creators:
Holmes, Kenneth C.1, Author           
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

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Free keywords: actin-tropomyosin binding; X-ray fiber diffraction; electrostatic interaction; radial and azimuthal position of tropomyosin; acto-myosin binding
 Abstract: We present a model of the actin-tropomyosin complex in which the radial and azimuthal position of tropomyosin was adjusted to fit the X-ray fiber diffraction patterns from oriented actin-tropomysin gels at a resolution of 1/8 Å−1. We used the recently published atomic F-actin model for the calculations. The atomic model of tropolyosin was obtained by model-building a coiled coiled-coil structure from the tropomyosin sequence. The resulting atomic model is strongly preferred and shows strong electrostatic interactions between charged side-chains of tropomyosin residues and actin residues in subdomain 3 and subdomain 4. Furthermore, calculations of enthalpies based upon electrostatic interactions indicate that there is a favored rotational position of the tropomyosin core at the calculated azimuthal and radial position given by the X-ray refinement. Rotations of the tropomyosin strand out of this position turn strongly attractive electrostatic interactions into repulsive forces. The resulting binding radius of 39 Å and the determined azimuthal position of tropomyosin are in good agreement with electron microscopy reconstructions and neutron diffraction experiments. Furthermore, the calculated position of tropomyosin would still partly block the rigor interaction of myosin cross-bridges with actin, whereas it very likely allows undisturbed binding of the cross-bridges in a weak binding state.

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Language(s): eng - English
 Dates: 1994-11-031994-09-081994-11-031995-02-10
 Publication Status: Issued
 Pages: 12
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 666724
DOI: 10.1006/jmbi.1994.0070
URI: http://www.sciencedirect.com/science/article/pii/S0022283684700702
Other: 4176
 Degree: -

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Title: Journal of Molecular Biology (London)
  Other : J Mol Biol
Source Genre: Journal
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Publ. Info: London : Academic Press
Pages: - Volume / Issue: 246 (1) Sequence Number: - Start / End Page: 108 - 119 Identifier: ISSN: 0022-2836
CoNE: https://pure.mpg.de/cone/journals/resource/954922646042