NMR in the Study of Enzyme Catalysis

  • H. Rüterjans
Conference paper
Part of the Colloquium der Gesellschaft für Biologische Chemie 23.–25. April 1981 in Mosbach/Baden book series (MOSBACH, volume 32)


In order to understand enzyme catalysis it is necessary to know the specific spatial arrangement of the active site amino acid side chains. By interaction with each other or with a coenzyme the functional groups of the active site form a sort of polar complex which enables the formation of the transition state of the enzyme substrate complex. However, because of the flexibility of the protein structure, equilibria of these manifold interactions have to be considered. If a distinct interaction between two side chains is needed for the catalytic activity, only the enzyme species with this interaction is active, whereas all other species should be inactive.


Imidazole Ring Amino Acid Side Chain Heme Group Bohr Effect Pancreatic Ribonuclease 
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Copyright information

© Springer-Verlag Berlin Heidelberg 1981

Authors and Affiliations

  • H. Rüterjans
    • 1
  1. 1.Institut für Biophysikalische Chemie der Johann Wolfgang Goethe-UniversitätFrankfurtGermany

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