Abstract
We use elastic neutron scattering to demonstrate that a sharp increase in the mean-squared atomic displacements, commonly observed in hydrated proteins above 200 K and often referred to as the dynamical transition, is present in the hydrated state of both native and denatured lysozyme. A direct comparison of the native and denatured protein thus confirms that the presence of the transition in the mean-squared atomic displacements is not specific to biologically functional molecules.
| Original language | English |
|---|---|
| Pages (from-to) | 291-297 |
| Number of pages | 7 |
| Journal | Journal of Biological Physics |
| Volume | 36 |
| Issue number | 3 |
| DOIs | |
| State | Published - Jun 2010 |
Funding
Acknowledgements The authors are thankful to K. W. Herwig and C. Hoffmann for critical reading of the manuscript, and K. L. Weiss for useful technical discussions. This work was supported by the US Department of Energy Basic Energy Sciences and the Office of Biological and Environmental Research, using facilities supported by Oak Ridge National Laboratory, and managed by UT-Battelle, LLC, for the US DOE under Contract No. DE-AC05-00OR22725.
| Funders | Funder number |
|---|---|
| U.S. Department of Energy | |
| Basic Energy Sciences | |
| Oak Ridge National Laboratory |
Keywords
- Biomolecules
- Dynamics
- Neutron scattering