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)


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.


Pyridoxal Phosphate Partial Assembly Isomerization Process Carbon Proton Thermodynamic Dissociation Constant 
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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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