Conformation Changes in the Assembly of the α2ß2 Complex Of Tryptophan Synthase

  • A. N. Lane
  • C. H. Paul
  • K. Kirschner
Conference paper
Part of the Nato Science Series A: (closed) book series (NSSA, volume 81)

Abstract

Many studies have addressed the question why most soluble enzymes are oligomeric (Welch, 1977, Friedman and Beychock, 1979; Jaenicke, 1982). By investigating the kinetics of refolding and reassociation of completely denatured proteins, and also testing the properties of folded but immobilized monomers it has been shown that assembly often modifies the intrinsic catalytic properties of monomers.

Keywords

Pyridoxal Phosphate Partial Assembly Isomerization Process Carbon Proton Thermodynamic Dissociation Constant 
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

© Springer Science+Business Media New York 1984

Authors and Affiliations

  • A. N. Lane
    • 1
  • C. H. Paul
    • 1
  • K. Kirschner
    • 1
  1. 1.Department of Biophysical ChemistryBiozentrum University of BaselBaselSwitzerland

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