Search Results - (Author, Cooperation:E. F. Pai)

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  1. 1
    H. W. Choe ; Y. J. Kim ; J. H. Park ; T. Morizumi ; E. F. Pai ; N. Krauss ; K. P. Hofmann ; P. Scheerer ; O. P. Ernst
    Nature Publishing Group (NPG)
    Published 2011
    Staff View
    Publication Date:
    2011-03-11
    Publisher:
    Nature Publishing Group (NPG)
    Print ISSN:
    0028-0836
    Electronic ISSN:
    1476-4687
    Topics:
    Biology
    Chemistry and Pharmacology
    Medicine
    Natural Sciences in General
    Physics
    Keywords:
    Binding Sites ; Conserved Sequence ; Crystallization ; Crystallography, X-Ray ; GTP-Binding Protein alpha Subunits/chemistry/metabolism ; Ligands ; Models, Molecular ; Opsins/chemistry ; Peptide Fragments/chemistry/metabolism ; Protein Conformation ; Retinaldehyde/chemistry/metabolism ; Rhodopsin/*chemistry/*metabolism ; Schiff Bases/chemistry ; Static Electricity
    Published by:
    http://www.nature.com/

    Latest Papers from Table of Contents or Articles in Press
  2. 2
    Schulz, G. E. ; Schirmer, R. H. ; Sachsenheimer, W. ; Pai, E. F.

    [s.l.] : Nature Publishing Group
    Published 1978
    Staff View
    ISSN:
    1476-4687
    Source:
    Nature Archives 1869 - 2009
    Topics:
    Biology
    Chemistry and Pharmacology
    Medicine
    Natural Sciences in General
    Physics
    Notes:
    [Auszug] The three-dimensional structure of the dimeric flavoenzyme glutathione reductase from human erythrocytes has been elucidated by an X-ray diffraction analysis at 0.3 nm resolution. The polypeptide chain has been traced, and the binding positions of FAD, NADP and glutathione have been determined. A ...
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1038/273120a0

    Articles: DFG German National Licenses
  3. 3
    Schiering, N. ; Kabsch, W. ; Moore, M. J. ; Distefano, M. D. ; Walsh, C. T. ; Pai, E. F.

    [s.l.] : Nature Publishing Group
    Published 1991
    Staff View
    ISSN:
    1476-4687
    Source:
    Nature Archives 1869 - 2009
    Topics:
    Biology
    Chemistry and Pharmacology
    Medicine
    Natural Sciences in General
    Physics
    Notes:
    [Auszug] The three-dimensional structure of MerA from Bacillus sp. strain RC607 can be clearly divided into three parts: the two N-terminal regions (residues 1-166), the core (167-616), the equivalent of the glutathione reductase structure, and the C-terminal extension (residues 617-631). This partition is ...
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1038/352168a0

    Articles: DFG German National Licenses