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Functional Significance of Flexibility in Proteins

  • Robert Huber
  • William S. BennettJr.
Conference paper

Abstract

The structural basis and the functional implications of large-scale flexibility are discussed for three systems: trypsin-trypsinogen, immunoglobulins, and citrate synthase. The trypsin-trypsinogen system provides an example in which an order-disorder transition is used as a means to regulate enzymatic activity. Immunoglobulins demonstrate how flexibility linked domains may be used to allow the binding of ligands with diverse arrangements. In citrate synthase, domain motion forms an active site that is shielded from solvent. Analogous large-scale flexibility has been observed in a number of other systems.

Keywords

Iron Atom Closed State Large Domain Rigid Body Movement Functional Implication 
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.

References

  1. R. Huber and W. S. Bennett (1983) Biopolymers 22, 261–279.CrossRefGoogle Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 1986

Authors and Affiliations

  • Robert Huber
    • 1
  • William S. BennettJr.
    • 1
  1. 1.Max-Placnk-Institut für BiochemieMartinsried bei MünchenFederal Republic of Germany

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