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Protein Engineering and Structure/Function Relations in Bovine Calbindin D9k

  • S. Forsén
  • T. Drakenberg
  • C. Johansson
  • S. Linse
  • E. Thulin
  • J. Kördel
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 269)

Abstract

In an attempt to elucidate the relationships between structure, dynamics and function in the calmodulin superfamily of Ca2+-binding intracellular proteins we have undertaken a detailed study of bovine calbindin D9k. This protein has a size (Mr≃8,500) and tertiary structure similar to that of the globular domains of calmodulin and troponin C and binds two Ca2+ -ions strongly (K ≃107 - 108 M-1, depending on the ionic strength). The schematic structure of the molecule is shown in figure 1.

Keywords

Mutant Protein Chemical Shift Difference Proton Pair Conformational Heterogeneity Sequence Specific Assignment 
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

© Plenum Press, New York 1990

Authors and Affiliations

  • S. Forsén
    • 1
  • T. Drakenberg
    • 1
  • C. Johansson
    • 1
  • S. Linse
    • 1
  • E. Thulin
    • 1
  • J. Kördel
    • 1
  1. 1.Physical Chemistry 2, Chemical CentreUniversity of LundLundSweden

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