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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Hyperfine interactions 29 (1986), S. 1395-1398 
    ISSN: 1572-9540
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract Melanosomes from bovine eyes have been studied by Mössbauer spectroscopy and X-ray diffraction as a function of temperature and of degree of hydration. The partially disordered structure of melanin is not modified by the interaction with the proteic matrix. The obtained values of 〈u2〉 indicate that high water contents stabilize the melanin structure, decreasing the amplitude of the atomic displacements.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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  • 2
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Biopolymers 23 (1984), S. 1481-1498 
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Measurements of Rayleigh scattering of Mössbauer radiation (RSMR) have been performed on synthetic L-Dopa melanin as a function of the scattering vector, Q, and temperature, T, and are compared with the results of X-ray diffraction analyses. The data obtained allow us to derive a radial distribution function for the atomic positions not affected by the dynamic disorder and determined only by the distribution of equilibrium interatomic distances. The mean-square atomic displacements, 〈u2〉, derived from the RSMR measurements, evidence a strong anisotropy of the atomic vibrations: even at room temperature, 〈u2〉 reaches fairly high values for off-plane displacements, as compared with those for motions within the planes of the structure. A connection is suggested between the observed dynamics and the biological screening action of melanins.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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