Browsing by Author "Smith, Jeremy C."
Now showing items 1-5 of 17
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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 ... -
Direct determination of vibrational density of states change on ligand binding to a protein
Balog, Erika; Becker, Torsten; Oettl, Martin; Lechner, Ruep; Daniel, Roy M.; Finney, John L.; Smith, Jeremy C. (American Physical Society, 2004)The change in the vibrational density of states of a protein (dihydrofolate reductase) on binding a ligand (methotrexate) is determined using inelastic neutron scattering. The vibrations of the complex soften significantly ... -
The dynamic transition in proteins may have a simple explanation
Daniel, Roy M.; Finney, John L.; Smith, Jeremy C. (Royal Society of Chemistry, 2003)The transition that has been observed in the dynamics of hydrated proteins at low temperatures (180–230 K) is normally interpreted as a change from vibrational, harmonic motion at low temperatures to anharmonic motions as ... -
Dynamics of immobilized and native Escherichia coli dihydrofolate reductase by quasielastic neutron scattering
Tehei, Moeava; Smith, Jeremy C.; Monk, Colin R.; Ollivier, Jacques; Oettl, Martin; Kurkal, Vandana; Finney, John L.; Daniel, Roy M. (Biophysical Society, 2006-10)The internal dynamics of native and immobilized Escherichia coli dihydrofolate reductase (DHFR) have been examined using incoherent quasielastic neutron scattering. These results reveal no difference between the high ... -
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 ...
Co-authors for Jeremy C. Smith
Jeremy C. Smith has 25 co-authors in Research Commons.
- Erika Balog
- Torsten Becker
- Marie-Claire Bellissent-Funel
- David Clement
- Roy M. Daniel
- Rachel V. Dunn
- Dominique Durand
- Michel Ferrand
- John L. Finney
- Jennifer A. Hayward
- Stephanie Hery
- Vandana Kurkal
- Ruep Lechner
- Lars Meinhold
- Colin R. Monk
- Martin Oettl
- Jacques Ollivier
- Michelle E. Peterson
- Stephanie Pouget
- Valerie Reat
- Mark A. Roberts
- Andrew Steer
- M. Tehei
- Moeava Tehei
- Alexander L. Tournier