Direct Observation of Correlated Interdomain Motion in Alcohol Dehydrogenase

Ralf Biehl, Bernd Hoffmann, Michael Monkenbusch, Peter Falus, Sylvain Préost, Rudolf Merkel, and Dieter Richter
Phys. Rev. Lett. 101, 138102 – Published 26 September 2008

Abstract

Interdomain motions in proteins are essential to enable or promote biochemical function. Neutron spin-echo spectroscopy is used to directly observe the domain dynamics of the protein alcohol dehydrogenase. The collective motion of domains as revealed by their coherent form factor relates to the cleft opening dynamics between the binding and the catalytic domains enabling binding and release of the functional important cofactor. The cleft opening mode hardens as a result of an overall stiffening of the domain complex due to the binding of the cofactor.

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  • Received 9 April 2008

DOI:https://doi.org/10.1103/PhysRevLett.101.138102

©2008 American Physical Society

Authors & Affiliations

Ralf Biehl1, Bernd Hoffmann2, Michael Monkenbusch1, Peter Falus3, Sylvain Préost4, Rudolf Merkel2, and Dieter Richter1

  • 1Institut für Festkörperforschung, Forschungszentrum Jülich, D-52425 Jülich, Germany
  • 2Institut für Bio- und Nanosysteme, Forschungszentrum Jülich, D-52425 Jülich, Germany
  • 3Institut Laue Langevin, F-38042 Grenoble, France
  • 4Hahn Meitner Institut, D-14109 Berlin, Germany

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Issue

Vol. 101, Iss. 13 — 26 September 2008

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