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Enzyme Activity and Flexibility at Very Low Hydration

V. Kurkal ^*, R. M. Daniel , John L. Finney , M. Tehei , R. V. Dunn  and Jeremy C. Smith ^*

^* Interdisciplinary Center for Scientific Computing (IWR), University of Heidelberg, D-69120 Heidelberg, Germany; Department of Biological Sciences, University of Waikato, Hamilton, New Zealand; and Department of Physics and Astronomy, University College London, London WC1E 6BT, England

Correspondence: Address reprint requests to Jeremy C. Smith, E-Mail: biocomputing{at}iwr.uni-heidelberg.de.

Recent measurements have demonstrated enzyme activity at hydrations as low as 3%. This raises the question of whether hydration-induced enzyme flexibility is important for activity. Here, to address this, picosecond dynamic neutron scattering experiments are performed on pig liver esterase powders at 0%, 3%, 12%, and 50% hydration by weight and at temperatures ranging from 120 to 300 K. At all temperatures and hydrations, significant quasielastic scattering intensity is found in the protein, indicating the presence of anharmonic, diffusive motion. As the hydration increases, a temperature-dependent dynamical transition appears and strengthens involving additional diffusive motion. The implication of these results is that, although the additional hydration-induced diffusive motion in the protein detected here may be related to increased activity, it is not required for the enzyme to function.

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