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  • 1
    Digitale Medien
    Digitale Medien
    The structure determination of the variable portion of the Bence-Jones protein Au (1975)
    Springer
    European biophysics journal 1 (1975), S. 139-146 
    Details
    ISSN: 1432-1017
    Schlagwort(e): Immunoglobulin ; Bence-Jones ; X-Ray ; Structure ; Rotation-Function ; Patterson Search ; Translation Function ; Molecular Replacement
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Physik
    Notizen: Abstract The structure of a χ-type Bence-Jones protein variable fragment Au has been determined by molecular replacement methods using the known structure of an other Bence-Jones variable fragment Rei (Epp et al., Eur. J. Biochem. 45, 513 (1974)). The crystallographic R factor is 0.31 for about 4000 significantly measured reflections between 6.8 to 2.5 å. The Au protein forms a dimer across a crystallographic two fold axis. The spatial relationship of the two monomers, the conformation of the backbones and of the internal residues is extremely similar to that found in Rei.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00539775
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Physicochemical and structural studies of phaseolin from French bean seed (1983)
    Springer
    Plant foods for human nutrition 33 (1983), S. 227-229 
    Details
    ISSN: 1573-9104
    Schlagwort(e): French bean ; Phaseolus vulgaris ; phaseolin ; seed globulin ; seed storage protein
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Land- und Forstwirtschaft, Gartenbau, Fischereiwirtschaft, Hauswirtschaft
    Notizen: Abstract Phaseolin, the main reserve globulin in seeds of the French bean (Phaseolus vulgaris L.), has been purified for sedimentation equilibrium analysis. The major protomer at neutral pH has a molecular weight of 150 000±5 000 which associates to a tetrameric form of molecular weight 596 000±20 000 at pH 4.5. The trimeric nature of the protomer is apparent from protein crosslinking experiments. Initial structural studies were made using optical rotatory dispersion and circular dichroism measurements. Two different crystal forms of the protein have been grown and characterised by X-ray diffraction; one of these forms appears suitable for high resolution X-ray analysis.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF01091313
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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