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Neutralization of Surface Charges Markedly Affects the Properties of Bovine Calbindin D9k

  • S. Forsén
  • M. Akke
  • P. Brodin
  • P. Bayley
  • T. Drakenberg
  • T. Grundström
  • C. Johansson
  • S. Linse
  • S. Martin
  • E. Thulin
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 255)

Abstract

Calbindin D9k constitutes an attractive model system for exploring the relationships between structure, dynamics and function in the EF-hand family of proteins. It is the smallest protein known (Mr ≈ 8,500; 75 a.a:s) with a pair of EF-hand Ca2+-binding sites and its structure resembles closely the globular domains of the homologous proteins calmodulin, parvalbumin and skeletal muscle troponin C. [1,7]. The schematic structure of calbindin is shown in Fig. 1.

Keywords

Surface Charge Urea Concentration Charge Amino Acid Loaded Form Attractive Model System 
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.

References

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Copyright information

© Plenum Press, New York 1989

Authors and Affiliations

  • S. Forsén
    • 1
  • M. Akke
    • 1
  • P. Brodin
    • 2
  • P. Bayley
    • 3
  • T. Drakenberg
    • 1
  • T. Grundström
    • 2
  • C. Johansson
    • 1
  • S. Linse
    • 1
  • S. Martin
    • 3
  • E. Thulin
    • 1
  1. 1.Physical Chemistry2, Chemical CentreLund UniversityLundSweden
  2. 2.Unit of Appl. Cell and Molecular BiologyUmeå UniversityUmeåSweden
  3. 3.Div. of Physical BiochemistryNatl. Institute for Medical ResearchMill Hill, LondonEngland

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