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      Low frequency enzyme dynamics as a function of temperature and hydration: A neutron scattering study

      Kurkal, Vandana; Daniel, Roy M.; Finney, John L.; Tehei, M.; Dunn, Rachel V.; Smith, Jeremy C.
      DOI
       10.1016/j.chemphys.2005.05.019
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      Kurkal, V., Daniel, R.M., Finney, J.L., Tehei, M., Dunn, R.V. & Smith, J.C. (2005). Low frequency enzyme dynamics as a function of temperature and hydration: A neutron scattering study. Chemical Physics, 317(2-3), 267-273.
      Permanent Research Commons link: https://hdl.handle.net/10289/4443
      Abstract
      The effect of hydration and temperature on the low-frequency dynamics of the enzyme Pig liver esterase has been investigated with incoherent neutron scattering experiments. The results suggest that at low temperature, increasing hydration results in lower flexibility of the protein. At higher temperatures, systems containing sufficient number of water molecules interacting with the protein exhibit increased flexibility. The environmental force constants indicate that the environment of the protein is more rigid below than it is above the dynamical transition temperature.
      Date
      2005
      Type
      Journal Article
      Publisher
      Elsevier
      Collections
      • Science and Engineering Papers [3124]
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