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  • Condensed Matter: Structure, etc.  (1)
  • Cooperative phenomena  (1)
  • Proteins  (1)
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  • 1
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    High Contrast X-ray Speckle from Atomic-Scale Order in Liquids and Glasses (2012)
    American Physical Society (APS)
    Details
    Publication Date: 2012-11-03
    Description: Author(s): S. O. Hruszkewycz, M. Sutton, P. H. Fuoss, B. Adams, S. Rosenkranz, K. F. Ludwig, Jr., W. Roseker, D. Fritz, M. Cammarata, D. Zhu, S. Lee, H. Lemke, C. Gutt, A. Robert, G. Grübel, and G. B. Stephenson The availability of ultrafast pulses of coherent hard x rays from the Linac Coherent Light Source opens new opportunities for studies of atomic-scale dynamics in amorphous materials. Here, we show that single ultrafast coherent x-ray pulses can be used to observe the speckle contrast in the high-ang... [Phys. Rev. Lett. 109, 185502] Published Fri Nov 02, 2012
    Keywords: Condensed Matter: Structure, etc.
    Print ISSN: 0031-9007
    Electronic ISSN: 1079-7114
    Topics: Physics
    Published by American Physical Society (APS)
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  • 2
    Electronic Resource
    Electronic Resource
    Cooperative Conformational Changes in Globular Proteins (1972)
    Weinheim : Wiley-Blackwell
    Angewandte Chemie International Edition in English 11 (1972), S. 894-906 
    Details
    ISSN: 0570-0833
    Keywords: Cooperative phenomena ; Conformation analysis ; Proteins ; Rearrangement ; Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: In globular proteins, the complicated steric arrangement of the polypeptide chain is determined by several interdependent cooperative interactions. These macromolecules are capable of reacting to changes in the environmental conditions such as temperature and pressure or the concentration of a wide range of compounds by changing their conformation and hence their biological and chemical properties. They are thus suitable for regulation processes or information storage in solution with a wide range of time constants. Environmental effects of this kind can be followed and explained in part at the molecular level by investigation of the time-dependent reversible unfolding of a number of proteins that can be described to a good approximation by a strongly cooperative “all-or-none” transition between two states.
    Additional Material: 13 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/anie.197208941
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