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  • 1
    Electronic Resource
    Electronic Resource
    Location of the ATPase site of myosin determined by three-dimensional electron microscopy (1987)
    [s.l.] : Nature Publishing Group
    Nature 329 (1987), S. 635-638 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Until now only X-ray crystallography has been able to show the three-dimensional location of functional sites of proteins. We report here an alternative approach13 combining the use of three-dimensional image reconstruction from electron microscopy4'11 and site-specific labelling with the ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/329635a0
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  • 2
    Electronic Resource
    Electronic Resource
    Swing of the lever arm of a myosin motor at the isomerization and phosphate-release steps (1998)
    [s.l.] : Macmillan Magazines Ltd.
    Nature 396 (1998), S. 380-383 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] In muscle, the myosin head (‘crossbridge’) performs the ‘working stroke’, in which ATP is hydrolysed to generate the sliding of actin and myosin filaments. The myosin head consists of a globular motor domain and a long lever-arm domain. The ‘lever-arm ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/24640
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  • 3
    Electronic Resource
    Electronic Resource
    Three-dimensional structure of the kinesin headá¤-microtubule complex (1995)
    [s.l.] : Nature Publishing Group
    Nature 376 (1995), S. 274-277 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The MT surface has been decorated with K340 (ref. 9), which contains the 340 N-terminal residues of the mouse kinesin heavy chain10. Until now, studies of the three-dimensional structure of the kinesin head-MT complex have been limited9'11'12 because most MTs have a seam line along the ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/376274a0
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  • 4
    Electronic Resource
    Electronic Resource
    Structural change of crossbridges of rabbit skeletal muscle during isometric contraction (1993)
    Springer
    Journal of muscle research and cell motility 14 (1993), S. 432-445 
    Details
    ISSN: 1573-2657
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Structural changes of crossbridges during isometric contraction have been studied by electron microscopy. Chemically skinned rabbit fibres were rapidly frozen either in activating solution or in ATP-free (rigor) solution, freeze-substituted and embedded. Longitudinal sections of muscle fibres show that the number of crossbridges in active fibres (isometric contraction) is approximately the same as in rigor fibres. Crossbridges of the active and rigor states differ in their shapes, angles and manner of arrangement on the thin filaments. In rigor many crossbridges are wide near the thin filaments and narrow near the thick filament shafts; in active fibres they have more uniform width along their length. The angle of the crossbridges in active fibres is somewhat variable. The average angle is ∼90° to the filament axis. The crossbridges are arranged on the thin filament retaining the 14.3 nm thick filament periodicity. The crossbridges in rigor are tilted and their arrangement near the thin filament reveals the 36 nm actin periodicity. The variability in the shapes of the crossbridges in active fibres is still higher when we look at them in cross-sections of muscle fibres. The crossbridge shapes in the cross-sections were classified and the relative frequency of different shapes was determined. The shapes that are commonly observed in active fibres are similar in that the majority of the mass of the crossbridges is farther away from the thin filament than the crossbridges in rigor fibres.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00121295
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