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Protein Engineering of Elongation Factor Tu

  • M. Jensen
  • K. K. Mortensen
  • H. U. Petersen
  • T. F. M. la Cour
  • J. Nyborg
  • M. Kjeldgaard
  • S. Thirup
  • B. F. C. Clark
Part of the NATO ASI Series book series (NATO ASI, volume 169)

Summary

The general goal of our programme is to study how alterations in a protein’s structure can modify its biological function. The protein selected for study is the elongation factor EF-Tu. This was chosen because of its own fundamental biological importance, because of its recently-recognized significance as a member of a group of GTP-binding proteins of medical relevance, and finally because of existing experience and expertise with this protein in our laboratory. The long-term aim of our research programme is to study this factor with special reference to modification of its substrate specificity, its sensitivity towards antibiotics and its thermal stability. In this contribution, we shall look at the important property of EF-Tu that we have just alluded to, namely, its ability to bind specifically to the energy-rich substrate molecule GTP.

Keywords

GTPase Activity Protein Structure Determination Automate Data Collection Guanosine Nucleotide Phosphate Binding 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

© Plenum Press, New York 1989

Authors and Affiliations

  • M. Jensen
    • 1
  • K. K. Mortensen
    • 1
  • H. U. Petersen
    • 1
  • T. F. M. la Cour
    • 1
  • J. Nyborg
    • 1
  • M. Kjeldgaard
    • 1
  • S. Thirup
    • 1
  • B. F. C. Clark
    • 1
  1. 1.Division of Biostructural Chemistry, Department of ChemistryAarhus UniversityAarhus CDenmark

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