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The Influence of Solvent Composition on Global Dynamics of Human Butyrylcholinesterase Powders: A Neutron-Scattering Study

F. Gabel ^*, M. Weik ^*, B. P. Doctor , A. Saxena , D. Fournier , L. Brochier , F. Renault , P. Masson , I. Silman ^¶ and G. Zaccai ^* ||

^* Laboratoire de Biophysique Moléculaire, Institut de Biologie Structurale, Grenoble, France; Division of Biochemistry, Walter Reed Army Institute of Research, Silver Spring, Maryland; Institut de Pharmacologie et Biologie Structurale, Toulouse, France; Centre de Recherches du Service de Santé des Armées, Unité d'Enzymologie, La Tronche, France; ^¶ Department of Neurobiology, Weizmann Institute of Science, Rehovot, Israel; and ^|| Institut Laue-Langevin, Grenoble, France

Correspondence: Address reprint requests to G. Zaccai, Inst. de Biologie Structurale CEA-CNRS, 41 rue Jules Horowitz, F-38027 Grenoble Cedex 1, France. Tel.: 33-43-878-9573; E-mail: zaccai@ibs.fr.

A major result of incoherent elastic neutron-scattering experiments on protein powders is the strong dependence of the intramolecular dynamics on the sample environment. We performed a series of incoherent elastic neutron-scattering experiments on lyophilized human butyrylcholinesterase (HuBChE) powders under different conditions (solvent composition and hydration degree) in the temperature range from 20 to 285 K to elucidate the effect of the environment on the enzyme atomic mean-square displacements. Comparing D₂O- with H₂O-hydrated samples, we were able to investigate protein as well as hydration water molecular dynamics. HuBChE lyophilized from three distinct buffers showed completely different atomic mean-square displacements at temperatures above 200 K: a salt-free sample and a sample containing Tris-HCl showed identical small-amplitude motions. A third sample, containing sodium phosphate, displayed highly reduced mean-square displacements at ambient temperature with respect to the other two samples. Below 200 K, all samples displayed similar mean-square displacements. We draw the conclusion that the reduction of intramolecular protein mean-square displacements on an Ångstrom-nanosecond scale by the solvent depends not only on the presence of salt ions but also on their type.

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