Literature DB >> 19137674

[A comparison of the models of a thin filament in the muscle with low-angle X-ray diffraction data obtained for the relaxed rabbit muscle].

N A Kubasova.   

Abstract

The models of a thin filament based on different structures of G-actin and the modes of their packing into helical structure have been compared with the experimental data obtained on thin bundles of skeletal muscle fibres in the relaxed state. The contribution of the main components of the thin filament to the intensity of the actin layer lines was studied. The best fit to the observed actin layer lines was achieved with the new F-actin structure based on the latest model of actin monomer 3BYH.PDB.

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Year:  2008        PMID: 19137674

Source DB:  PubMed          Journal:  Biofizika        ISSN: 0006-3029


  3 in total

1.  The fraction of myosin motors that participate in isometric contraction of rabbit muscle fibers at near-physiological temperature.

Authors:  Andrey K Tsaturyan; Sergey Y Bershitsky; Natalia A Koubassova; Manuel Fernandez; Theyencheri Narayanan; Michael A Ferenczi
Journal:  Biophys J       Date:  2011-07-20       Impact factor: 4.033

2.  The Closed State of the Thin Filament Is Not Occupied in Fully Activated Skeletal Muscle.

Authors:  Sergey Y Bershitsky; Natalia A Koubassova; Michael A Ferenczi; Galina V Kopylova; Theyencheri Narayanan; Andrey K Tsaturyan
Journal:  Biophys J       Date:  2017-04-11       Impact factor: 4.033

3.  Tropomyosin movement is described by a quantitative high-resolution model of X-ray diffraction of contracting muscle.

Authors:  Natalia A Koubassova; Sergey Y Bershitsky; Michael A Ferenczi; Theyencheri Narayanan; Andrey K Tsaturyan
Journal:  Eur Biophys J       Date:  2016-09-17       Impact factor: 1.733

  3 in total

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