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      Enzyme activity and flexibility at very low hydration

      Kurkal, Vandana; Daniel, Roy M.; Finney, John L.; Tehei, Moeava; Dunn, Rachel V.; Smith, Jeremy C.
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      Biophy Hydration.pdf
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      DOI
       10.1529/biophysj.104.058677
      Link
       www.biophysj.org
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      Kurkal, V., Daniel, R. M., Finney, J. L., Tehei, M., Dunn, R. & Smith, J.C. (2005). Enzyme activity and flexibility at very low hydration. Biophysical Journal, 89, 1282- 1287.
      Permanent Research Commons link: https://hdl.handle.net/10289/1286
      Abstract
      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.
      Date
      2005-05
      Type
      Journal Article
      Publisher
      Biophysical Society
      Rights
      This article has been published in the journal: Biophysical Journal. Copyright © 2005 by the Biophysical Society.
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      • Science and Engineering Papers [3124]
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