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  • 1
    Electronic Resource
    Electronic Resource
    X-Ray Diffraction Studies of Muscle (1981)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Physiology 43 (1981), S. 553-565 
    Details
    ISSN: 0066-4278
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Medicine , Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.ph.43.030181.003005
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  • 2
    Electronic Resource
    Electronic Resource
    STRUCTURAL MECHANISM OF MUSCLE CONTRACTION (1999)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Biochemistry 68 (1999), S. 687-728 
    Details
    ISSN: 0066-4154
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Chemistry and Pharmacology , Biology
    Notes: Abstract X-ray crystallography shows the myosin cross-bridge to exist in two conformations, the beginning and end of the "power stroke." A long lever-arm undergoes a 60o to 70o rotation between the two states. This rotation is coupled with changes in the active site (OPEN to CLOSED) and phosphate release. Actin binding mediates the transition from CLOSED to OPEN. Kinetics shows that the binding of myosin to actin is a two-step process which affects ATP and ADP affinity. The structural basis of these effects is not explained by the presently known conformers of myosin. Therefore, other states of the myosin cross-bridge must exist. Moreover, cryoelectronmicroscopy has revealed other angles of the cross-bridge lever arm induced by ADP binding. These structural states are presently being characterized by site-directed mutagenesis coupled with kinetic analysis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.biochem.68.1.687
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  • 3
    Electronic Resource
    Electronic Resource
    Computer processing and analysis of X-ray fibre diffraction data (1993)
    Copenhagen : International Union of Crystallography (IUCr)
    Applied crystallography online 26 (1993), S. 82-91 
    Details
    ISSN: 1600-5767
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Geosciences , Physics
    Notes: The processing and analysis of fibre diffraction data is often cumbersome. Presented here is a compact interactive computer program, PROFIDA (processing of fibre diffraction data), for fast processing of fibre diffraction data from biological molecules without many of the difficulties. Interactive rotation and centring of the diffraction pattern allow four-quadrant averaging and background subtraction. Furthermore, film coordinates may be transformed into reciprocal-space coordinates for any orientation of the specimen. Specimen tilt towards the incident-beam direction may be determined and the appropriate correction made. In addition, a routine that scales and merges data sets from a film pack is available. Data analysis is supported by an integration routine that allows layer-line profiles to be examined and integrated and layer-line plots to be produced under control of the cursor. The program is written in C to run on the Silicon Graphics Iris workstation with a button-and-dial box using the Iris graphics library.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0021889892008781
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    The effect of disorientation on the intensity distribution of non-crystalline fibres. I. Theory (1974)
    [S.l.] : International Union of Crystallography (IUCr)
    Acta crystallographica 30 (1974), S. 635-638 
    Details
    ISSN: 1600-5724
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The intensity function in reciprocal space is derived for the case of non-crystalline fibres with a Gaussian distribution of orientations. An expression is found relating the observed intensity function with the weighted integral along a circle of the intensity derived from the molecular structure factor. From this result in the case where the layer-line width is very small a correction factor may be derived which, if applied to the observed intensity, yields the intensity which would be obtained from a perfectly orientated fibre. The general problem of correcting for disorientation can only be treated by a numerical deconvolution procedure.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0567739474001537
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    Paper (German National Licenses)
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  • 5
    Electronic Resource
    Electronic Resource
    Structural evidence that myosin heads may interact with two sites on F-actin (1982)
    [s.l.] : Nature Publishing Group
    Nature 299 (1982), S. 467-469 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Optical diffraction patterns from electron microscope (EM) images of different filaments show variation in the positions of intensity peaks along the layer lines, presumably because of distortions induced during staining and dehydration. For example, the radial positions of the strongest peaks on ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/299467a0
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  • 6
    Electronic Resource
    Electronic Resource
    Unusual segmental flexibility in a region of tobacco mosaic virus coat protein (1978)
    [s.l.] : Nature Publishing Group
    Nature 273 (1978), S. 564-566 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Fig. 1 JH NMR spectra of TMV coat protein at 360 MHz. Protein concentration 10 mg ml"1 in phosphate buffer F/2 = 0.1, temperature 27 C, pH as indicated, a, 4S particle, pH 8.5; b, disk (19-22S), pH 7.1; c, helix (〉 30S), pH 6.0. Chemical shifts (5) in p.p.m. from internal DSS. AR = Aromatic ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/273564a0
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    Paper (German National Licenses)
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  • 7
    Electronic Resource
    Electronic Resource
    Synchrotron Radiation as a Source for X-ray Diffraction (1971)
    [s.l.] : Nature Publishing Group
    Nature 230 (1971), S. 434-437 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Some preliminary results have been obtained with synchrotron radiation from the 7.5 GeV electron synchrotron Deutsches Elektronen - Synchrotron (DESY) in Hamburg as a source for X-ray ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/230434a0
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  • 8
    Electronic Resource
    Electronic Resource
    Structure of tobacco mosaic virus at 6.7 Å resolution (1975)
    [s.l.] : Nature Publishing Group
    Nature 254 (1975), S. 192-196 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The electron density distribution of tobacco mosaic virus has been determined to 6.7 Å resolution by analysis of the X-ray diffraction pattern given by oriented gels of the virus. This has been achieved by separation of overlapping Bessel function terms by a technique analogous to ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/254192a0
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  • 9
    Electronic Resource
    Electronic Resource
    Crystallization of Transfer RNA (1968)
    [s.l.] : Nature Publishing Group
    Nature 219 (1968), S. 1222-1224 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] A bacterial transfer RNA (tRNAFMet) has been obtained in micro-crystalline form. Its probable unit cell dimensions have been deduced from X-ray powder ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/2191222a0
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  • 10
    Electronic Resource
    Electronic Resource
    Constancy of Axial Spacings in Frog Sartorius Muscle during Contraction (1965)
    [s.l.] : Nature Publishing Group
    Nature 206 (1965), S. 1358-1358 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] It is of great importance for theories of contraction to know whether changes in the internal configuration of the actin or myosin filaments occur between the resting and the active state of the muscle. Much information from electron-microscopy indicates that overall changes in filament lengths do ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/2061358a0
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