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Coherent intramolecular dynamics in populations of allosteric enzymes

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Book cover Transport and Structure

Part of the book series: Lecture Notes in Physics ((LNP,volume 532-532))

Abstract

The diffusive transport and mixing times of regulatory molecules in micrometer and sub-micrometer reaction volumes can be shorter than characteristic times of conformational transformations in single enzyme molecules. Under these conditions, mutual synchronization of individual molecular turnover cycles takes place when strong allosteric activation by the reaction products is present. Using simple automaton models to describe the cycles of single molecules, we analyze properties of the synchronization transition.

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Author information

Author notes

  1. Benno Hess

    Present address: Max-Planck-Institut für medizinische Forschung, Jahnstraße 29, D-69120, Heidelberg, Germany

Authors and Affiliations

  1. Abteilung Physikalische Chemie, Fritz-Haber-Institut der Max-Planck-Gesellschaft, Faradayweg 4–6, D-14195, Berlin (Dahlem), Germany

    Pedro Stange & Alexander S. Mikhailov

  2. Max-Planck-Institut für molekulare Physiologie, Otto-Hahn-Str. 11, D-44227, Dortmund, Germany

    Benno Hess

Authors
  1. Pedro Stange
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  2. Alexander S. Mikhailov
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  3. Benno Hess
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Editor information

Stefan C. Müller Jürgen Parisi Walter Zimmermann

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© 1999 Springer-Verlag

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Stange, P., Mikhailov, A.S., Hess, B. (1999). Coherent intramolecular dynamics in populations of allosteric enzymes. In: Müller, S.C., Parisi, J., Zimmermann, W. (eds) Transport and Structure. Lecture Notes in Physics, vol 532-532. Springer, Berlin, Heidelberg. https://doi.org/10.1007/BFb0104229

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  • DOI: https://doi.org/10.1007/BFb0104229

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  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-540-66632-5

  • Online ISBN: 978-3-540-48070-9

  • eBook Packages: Springer Book Archive

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