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  • 1990-1994  (5)
  • 1970-1974  (3)
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Year
  • 1
    Electronic Resource
    Electronic Resource
    Kinetics of interaction of HIV reverse transcriptase with primer/template (1993)
    s.l. : American Chemical Society
    Biochemistry 32 (1993), S. 7966-7971 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00082a018
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Thiophosphate analogs of nucleoside di- and triphosphates (1971)
    s.l. : American Chemical Society
    Journal of the American Chemical Society 93 (1971), S. 6252-6257 
    Details
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ja00752a042
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Light as a trigger for time-resolved structural experiments on muscle, lipids, p21 and bacteriorhodopsin (1991)
    Copenhagen : International Union of Crystallography (IUCr)
    Applied crystallography online 24 (1991), S. 857-865 
    Details
    ISSN: 1600-5767
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Geosciences , Physics
    Notes: With the availability of synchrotron-radiation facilities, new approaches to time-resolved structural experiments in biology have been developed. The common feature of the experiments described is the use of powerful light sources to trigger structural transitions by flash photolysis, flash excitation or laser temperature jump. Special emphasis will be given to the selection criteria for a laser temperature jump system and to the performance of the selected erbium glass laser as a tool for rapid temperature jumps. Experiments are presented on the structure and kinetics of muscle contraction, lipid phase transition, Ha-ras p21 Laue crystallography and structural changes during the photocycle of bacteriorhodopsin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0021889890013176
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Crystallographic studies on p21H−ras using the synchrotron Laue method: improvement of crystal quality and monitoring of the GTPase reaction at different time points (1994)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 50 (1994), S. 512-520 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The parameters affecting the crystal quality of complexes between p21H-ras and caged GTP have been investigated. The use of pure diastereomers of caged GTP complexed to the more stable p21(G12P)′ mutant of p21 and the addition of n-octyl-β-D-glucopyranoside improved the reproducibility and decreased the mosaicity of the crystals significantly. Furthermore, the crystallization technique was changed from the batch method to the sitting-drop technique. With the availability of a larger yield of well ordered crystals, it was possible to extend the time-resolved crystallographic investigations on p21H-ras. A structure of p21(G12P)′:GTP could be obtained 2 min after photolytic removal of the cage group and led to the identification of a previously unidentified conformation for the so-called catalytically active loop L4. The refinement of five data sets collected within 2 min at different times (2–4, 11–13, 20–22, 30–32 and 90–92 min) after the initiation of the intrinsic GTPase reaction of the protein indicates that the synchrotron Laue method can be used to detect small structural changes and alternative conformations, but is presently limited in the analysis of larger rearrangements since these produce diffuse and broken electron density.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S090744499301443X
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  • 5
    Electronic Resource
    Electronic Resource
    Crystallization and preliminary X-ray structure analysis of thermally unstable p21H−ras guanosine complexes (1994)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 50 (1994), S. 521-526 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: p21 is a small guanine nucleotide binding protein that is involved in intracellular signal transduction. Biochemical data suggest that the presence of the β-phosphate is essential for strong binding of guanine nucleotides to the protein. Guanosine or GMP bind six orders of magnitude more weakly to p21 than GDP or GTP. Moreover, the thermal stability of the protein is dramatically reduced when bound to GMP or guanosine. We have crystallized C-terminally truncated forms of p21H-ras, with guanosine or GMP bound, in the space groups P43212, P21212 and P21. The crystals diffract in the range 2.8–2.2 Å. Details of the crystallization procedures, the characterization of the crystals and preliminary results of structure determination are described. An unexpected electron-density peak was found close to the position of the β-phosphate in the phosphate-binding loop.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444994001253
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  • 6
    Electronic Resource
    Electronic Resource
    Time-resolved X-ray diffraction studies on stretch-activated insect flight muscle (1991)
    Springer
    Journal of muscle research and cell motility 12 (1991), S. 208-215 
    Details
    ISSN: 1573-2657
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The specific feature of stretch activation of the indirect flight muscle of the tropical waterbugLethocerus was used to correlate mechanical and structural aspects of muscle contraction. The time courses of the changes in intensities of the strongest equatorial reflections, the (10) and (20) and of the first meridional reflection at 14.5 nm−1 were monitored using synchrotron radiation as a high intensity X-ray source. The ratio of the intensities of the equatorial reflections, (I20/I10), which reflects the mass distribution within the filament lattice array, increases by about 10% relative to the Ca2+-activated level when a rapid stretch is imposed, compared with a 200% change seen when fibres change from the relaxed to the rigor state, while the spacing of the lattice planes decreases by about 1%. The intensity of the first meridional reflection at 14.5 nm−1 decreases by about 35% during stretch activation with a slightly faster time course than the delayed tension increase. The results suggest that the average structure of cycling crossbridges is different from that present in the rigor state.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01774040
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    Paper (German National Licenses)
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  • 7
    Electronic Resource
    Electronic Resource
    The molecular basis of contractility Part I (1974)
    Springer
    Basic research in cardiology 69 (1974), S. 88-104 
    Details
    ISSN: 1435-1803
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Muscular contraction stems from a sliding movement of thick and thin filaments relative to each other. These filaments run parallel to the direction of the muscle fibre. The thin filaments, which issue from the Z-membrane into the sarcomere, consist of 60% actin, and 40% regulator proteins (tropomyosin and troponin). The thick filament consists almost entirely of myosin. The two types of filaments form on overlapping region, the length of which depends on the degree of shortening of the muscle. The mechanical work which is produced by the muscle during shortening is produced by the so-called myosin cross-bridges, which appear to attach to actin, change their angle, and then detach in a cyclical “rowing-boat” manner. During such a cycle, ATP is split to ADP and inorganic phosphate, and therefore the production of mechanical work is based on the interaction of actin and myosin at the expense of chemical energy, which is supplied in the form of ATP. In the last 20 years, the structure of the involved proteins and their aggregation and ordering in the filaments has been widely investigated. Similarly, the rough nature of the electromechanical coupling process has been explained. i. e. the sequence of events which is necessary to activate a resting muscle into contraction via a neural impulse. At the present time, much interest is concentrated on the kinetic analysis of ATP hydrolysis and the modification of certain reaction steps by actin. From experiments of this sort, a more detailed and propound understanding of the nature of the mechanochemical energy coupling mechanism can be expected.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01910790
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  • 8
    Electronic Resource
    Electronic Resource
    The molecular basis of contractility Part II (1974)
    Springer
    Basic research in cardiology 69 (1974), S. 204-213 
    Details
    ISSN: 1435-1803
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Zusammenfassung Die Muskelkontraktion beruht auf dem aneinander-vorbei-Gleiten von dicken und dünnen Filamenten, die innerhalb der Muskelzelle parallel zur Faserrichtung verlaufen. Die dünnen Filamente, die von der Z-Linie ausgehend in die Sarkomere reichen, bestehen zu 60% aus dem Protein Aktin und zu 40% aus den Regulatorproteinen Tropomyosin und Tropomin. Das dicke Filament ist fast ausschließlich aus dem Protein Myosin aufgebaut. Beide Filamenttypen bilden eine Überlappungszone, deren Breite vom Ausmaß der Verkürzung der Muskelzelle abhängig ist. Die mechanische Kraft, die notwendig ist, um die beiden Filamente aneinander vorbeizutreiben, wird von der s. g. Myosinquerbrücke erzeugt, die in einer Art Ruderbewegung sich zyklisch am Aktinfilament anheftet, umknickt und wieder losläßt. Während dieses Vorgangs wird ATP zu ADP und anorganischem Phosphat vom Myosin hydrolysiert. Der molekulare Vorgang der Kraftgeneration innerhalb der Muskelzelle beruht somit auf der Interaktion der beiden Proteine Aktin und Myosin bei Verbrauch von chemischer Energie, die in Form von ATP vorliegt. In den letzten 20 Jahren ist die Struktur der beteiligten Proteine, die Art ihrer Aggregation in den Filamenten und die relative Anordnung der Filamente zueinander eingehend erforscht worden. Ebenfalls in groben Zügen ist auf molekularer Ebene der elektromechanische Koppelungsvorgang geklärt, d. h. die Sequenz von Vorgängen, die nötig sind, einen Muskel in Ruhe durch einen neuralen Impuls in einen sich aktiv verkürzenden zu verwandeln. Im Augenblick konzentriert sich das Interesse auf die kinetische Analyse der Hydrolyse des ATPs durch Myosin und den modifizierenden Einfluß des Aktins auf bestimmte Reaktionsschritte der ATP-Bindung und Spaltung am Myosin. Von derartigen Untersuchungen ist ein tieferer Einblick in den Vorgang der chemotechnischen Energieumwandlung auf molekularer Ebene zu erwarten.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01906200
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