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Nuclear Magnetic Resonance Studies of the Interaction of Lanthanide Cations with Lysozyme

  • C. M. Dobson
  • R. J. P. Williams
Part of the The Jerusalem Symposia on Quantum Chemistry and Biochemistry book series (JSQC, volume 9-1)

Abstract

Hen egg-white lysozyme is a small protein which consists of a single polypeptide chain of 129 amino acid residues, and has a molecular weight of ca. 14 400. Recent reviews (Imoto et al., 1972; Osserman et al., 1974) summarise the properties of the protein. It promotes the dissolution of bacterial cell walls, and is able to catalyse the hydrolyses of β-1,4-glycosidic linkages between residues in the polysaccharide components of the cell walls. The three-dimensional structure of the protein in the solid state has been determined, and a model of the structure constructed (Blake et al., 1967). This model shows that the molecule is roughly ellipsoidal in shape, with dimension about 45 × 30 × 30 Å. The molecule has a deep cleft on one side, divided into six sites A–F in which polysaccharide inhibitors and substrates bind. Two catalytically important ionisable groups are the carboxylic acid groups of glu 35 and asp 52 situated between sites D and E. The X-ray structure of the active site cleft is shown in Figure 1.

Keywords

Titration Curve Effective Distance Lanthanide Cation Active Site Cleft Weak Site 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© D. Reidel Publishing Company 1977

Authors and Affiliations

  • C. M. Dobson
    • 1
  • R. J. P. Williams
    • 1
  1. 1.Inorganic Chemistry LaboratoryOxfordEngland

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