Browsing by Author "Dunn, Rachel V."

Now showing items 1-5 of 13

  • Cryosolvents useful for protein and enzyme studies below −100°C

    Reat, Valerie; Finney, John L.; Steer, Andrew; Roberts, Mark A.; Smith, Jeremy C.; Dunn, Rachel V.; Peterson, Michelle E.; Daniel, Roy M. (Elsevier, 2000)
    For the study of protein structure, dynamics, and function, at very low temperatures it is desirable to use cryosolvents that resist phase separation and crystallisation. We have examined these properties in a variety of ...

  • Enzyme activity and dynamics: xylanase activity in the absence of fast anharmonic dynamics

    Dunn, Rachel V.; Reat, Valerie; Finney, John L.; Ferrand, Michel; Smith, Jeremy C.; Daniel, Roy M. (2000)
    The activity and dynamics of a simple, single subunit enzyme, the xylanase from Thermotoga maritima strain Fj SS3B.1 have been measured under similar conditions, from -70 to +10 °C. The internal motions of the enzyme, as ...

  • Enzyme activity and flexibility at very low hydration

    Kurkal, Vandana; Daniel, Roy M.; Finney, John L.; Tehei, Moeava; Dunn, Rachel V.; Smith, Jeremy C. (Biophysical Society, 2005-05)
    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 ...

  • Enzyme activity below the dynamical transition at 220 K

    Daniel, Roy M.; Smith, Jeremy C.; Ferrand, Michel; Hery, Stephanie; Dunn, Rachel V.; Finney, John L. (1998-11)
    Enzyme activity requires the activation of anharmonic motions, such as jumps between potential energy wells. However, in general, the forms and time scales of the functionally important anharmonic dynamics coupled to motion ...

  • Enzyme activity down to −100°C

    Bragger, J.M.; Dunn, Rachel V.; Daniel, Roy M. (Elsevier, 2000)
    The activities of two enzymes, beef liver catalase (EC 1.11.1.6) and calf intestine alkaline phosphatase (EC 3.1.3.1), have been measured down to −97°C and −100°C, respectively. Enzyme activity has not previously been ...

Co-authors for Rachel V. Dunn

Supervised by Rachel V. Dunn

Showing up to 5 theses - most recently added to Research Commons first.

  • Evidence for a third thermal parameter of enzymes

    Peterson, Michelle E. (The University of Waikato, 2005)
    This thesis describes tests of a new hypothesis describing the effect of temperature on enzyme activity. Traditionally, the dependence of enzyme activity on temperature has been described by a model (the 'Classical Model') ...