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The Enzyme Catalysis Process pp 103–122Cite as

Low Frequency Dynamics of Proteins Studied by Inelastic Neutron Scattering

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Part of the book series: Progress in Mathematics ((NSSA))

Abstract

In order to perform their biological function many proteins need to be able to adopt two or more different conformations and are induced to change from one to another by ligand or substrate binding or by a change in environmental conditions such as pH [1,2,3]. In several cases the nature of such conformational changes has been revealed by X-ray crystallography and shown to range from subtle reorientations of a few sidechains, to displacements of loops (e.g. phosphorylase, triose phosphate isomerase), pseudo-rigid body inter-domain motions (e.g. hexokinase, phosphoglycerate kinase [4]), subunit reorientations (heamoglobin, aspatate-transcarbamylase) and drastic rearrangements of the whole protein (e.g. influenza virus hemagglutinin). Conformational change or functional flexibility of this kind clearly involves internal protein motion. However there is overall direction to the motion and it is usually reversible.

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Authors and Affiliations

  1. Grenoble Outstation, European Molecular Biology Laboratory, c/o ILL, 156X, 38042, Grenoble, France

    Stephen Cusack

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  1. Stephen Cusack
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Editors and Affiliations

  1. Dept. of Chemistry, University of Glasgow, G12 8QQ, Glasgow, Scotland, UK

    Alan Cooper

  2. Istituto di Chimica Quantistica ed Energetica Molecolare, CNR, Via Risorgimento 35, I-56100, Pisa, Italy

    Julien L. Houben  & Lisa C. Chien  & 

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Cusack, S. (1989). Low Frequency Dynamics of Proteins Studied by Inelastic Neutron Scattering. In: Cooper, A., Houben, J.L., Chien, L.C. (eds) The Enzyme Catalysis Process. Progress in Mathematics. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-1607-8_9

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  • DOI: https://doi.org/10.1007/978-1-4757-1607-8_9

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4757-1609-2

  • Online ISBN: 978-1-4757-1607-8

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