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  • 1
    Electronic Resource
    Electronic Resource
    Thermal expansion of a protein (1987)
    s.l. : American Chemical Society
    Biochemistry 26 (1987), S. 254-261 
    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/bi00375a035
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    A reduction of protein specific motions in co-ligated myoglobin embedded in a trehalose glass (1998)
    Springer
    European biophysics journal 27 (1998), S. 173-176 
    Details
    ISSN: 1432-1017
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002490050123
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Ligand binding and conformational motions in myoglobin (2000)
    [s.l.] : Macmillian Magazines Ltd.
    Nature 404 (2000), S. 205-208 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Myoglobin, a small globular haem protein that binds gaseous ligands such as O2, CO and NO reversibly at the haem iron, serves as a model for studying structural and dynamic aspects of protein reactions. Time-resolved spectroscopic measurements after photodissociation of the ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/35004622
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  • 4
    Electronic Resource
    Electronic Resource
    Experimental test of a new method for phase determination using gamma resonance spectroscopy (1971)
    Springer
    The European physical journal 244 (1971), S. 456-467 
    Details
    ISSN: 1434-601X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract We have performed an experimental study of the feasability to employ resonance scattering of γ-radiation in order to measure directly the phase of the structure factor which is required in X-ray crystal structure determination. The phases of the (020) and the (040) reflection of a K3Fe(CN)6 single crystal were determined by measuring the interference between nuclear resonance scattering and by electronic scattering.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01400754
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  • 5
    Electronic Resource
    Electronic Resource
    Protein structural dynamics as determined by Mössbauer spectroscopy (1988)
    Springer
    Hyperfine interactions 40 (1988), S. 147-157 
    Details
    ISSN: 1572-9540
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract Mössbauer spectroscopy on57Fe allows the study of dynamics with a characteristic time faster 100 ns. For myoglobin a detailed physical picture of protein dynamics has been obtained. A myoglobin molecule has no well defined energy minimum. X-ray structure analysis yields only an average conformation. At low temperatures the molecules are trapped in slightly different structures called conformational substates. At higher temperatures a Brownian type of oscillation of molecular segments in restricted space occurs. RSMR technique allows an estimation of the characteristic size of these segments which are in myoglobin well below 30 A and larger than 6 A. A determination of the quasielastic absorption with high accuracy yields the energy distribution of the conformational substates. As further examples bacteriorhodopsin and a model compound for membranes are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02049086
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  • 6
    Electronic Resource
    Electronic Resource
    Protein dynamics studied on myoglobin (1999)
    Springer
    Hyperfine interactions 123-124 (1999), S. 825-840 
    Details
    ISSN: 1572-9540
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract Two methods of inelastic scattering of synchrotron radiation were used to measure the dynamics of myoglobin in the temperature range from T = 60 K to 300 K. The inelastic Rayleigh scattering of metmyoglobin was analyzed by delayed elastic nuclear forward scattering of an iron foil. This yields averaged information on all phonons within the sample. The mean square displacement of the atoms due to this dynamics is 〈x〉 2/T = 2.1 · 10—4 Å2 K—1 on average. Complementary information was obtained by phonon assisted nuclear scattering on deoxymyoglobin. This method selects the phonons coupling to the iron atom in the active center of the protein. The mean square displacement of the iron was measured to be 〈x〉 2/T = 0.6· 10—4 Å2 K—1. The results are in agreement with Mössbauer absorption experiments in the low temperature range. Above 200 K the results allow one to distinguish between harmonic and quasidiffusive dynamics within the protein. A comparison with Raman spectroscopy is made.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1017004814164
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  • 7
    Electronic Resource
    Electronic Resource
    The different iron binding sites of bovine spleen purple acid phosphatase (1988)
    Springer
    Hyperfine interactions 42 (1988), S. 885-888 
    Details
    ISSN: 1572-9540
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract The purple acid phosphatase contains two inequivalent irons which can be removed subsequently. The Mössbauer spectrum of the purple inactive enzyme (oxidized) indicates two high spin ferric irons with antiparallel coupling giving zero effective spin. The active pink enzyme (partly reduced) is obtained by a one electron transfer to the iron which is less stable bound in the protein. The Mössbauer spectra indicate a high spin Fe(2+) antiparallel spin coupled to high spin Fe(3+).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02395531
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  • 8
    Electronic Resource
    Electronic Resource
    The Mössbauer effect and collective motions in glass-forming liquids and polymeric networks (1994)
    Springer
    Hyperfine interactions 90 (1994), S. 243-264 
    Details
    ISSN: 1572-9540
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract Glass-forming liquids, synthetic polymers and biopolymers share essential properties. Dynamic processes in these complex systems are characterized by cooperative motions with wide distributions of time scales, which manifest themselves in broad quasielastic lines in the Mössbauer spectrum. In this article, the application of the Mössbauer effect to the study of structural dynamics in complex systems is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02069131
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  • 9
    Electronic Resource
    Electronic Resource
    Inter- and intramolecular motions in proteins (1992)
    New York, NY : Wiley-Blackwell
    International Journal of Quantum Chemistry 42 (1992), S. 1491-1498 
    Details
    ISSN: 0020-7608
    Keywords: Computational Chemistry and Molecular Modeling ; Atomic, Molecular and Optical Physics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The use of 57Fe Mössbauer radiation allows the study of protein crystal dynamics by a time-resolved analysis of X-ray scattering. In myoglobin cystals, the main source of the root mean squared amplitude of motions comes from intramolecular protein dynamics. Segments of the size of an α-helix move collectively. Long-range correlated motions give only a minor contribution. Comparison with Mössbauer absorption spectroscopy shows that protein-specific dynamics is frozen out below 200 K and the lattice dynamics is mainly responsible for the low-temperature behavior.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/qua.560420523
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  • 10
    Electronic Resource
    Electronic Resource
    Density distributions in the water shell of myoglobin (1996)
    New York, NY : Wiley-Blackwell
    International Journal of Quantum Chemistry 59 (1996), S. 263-269 
    Details
    ISSN: 0020-7608
    Keywords: Computational Chemistry and Molecular Modeling ; Atomic, Molecular and Optical Physics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Two different approaches were used to explain the distribution of water coordinates in the crystallographically invisible part of the unit cell. Monte Carlo calculations were done starting from different initial water structures. Extended Monte Carlo calculations using equal initial structures were also used to obtain two further water structures. The differences between the Monte Carlo water structures were used to calculate the mean-square displacements of the water molecules. Monte Carlo calculations starting from different structures lead to a mean-square displacement of 0.58 Å2, whereas extended Monte Carlo moves using the same initial structure only show a mean-square displacement of 0.17 Å2. The mean-square displacement of 0.58 Å2 can be used to explain the experimental data. © 1996 John Wiley & Sons, Inc.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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