Published June 1, 2010
| Version v1
Journal article
Dynamical Transition in Hydrated Biomolecules, Native and Denatured
Creators
- 1. Oak Ridge National Laboratory, TN (United States)
Description
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.
Additional details
Identifiers
Publishing Information
- Journal Title
- Journal of Biological Physics
- Journal Volume
- 36
- Journal Issue
- 3
- Journal Page Range
- p. 291-297
- ISSN
- 0092-0606
INIS
- Country of Publication
- United States
- Country of Input or Organization
- United States
- INIS RN
- 41078116
- Subject category
- S73: NUCLEAR PHYSICS AND RADIATION PHYSICS;
- Descriptors DEI
- ATOMIC DISPLACEMENTS; LYSOZYME; NEUTRONS; PROTEINS; SCATTERING
- Descriptors DEC
- BARYONS; ELEMENTARY PARTICLES; ENZYMES; FERMIONS; GLYCOSYL HYDROLASES; HADRONS; HYDROLASES; NUCLEONS; O-GLYCOSYL HYDROLASES; ORGANIC COMPOUNDS; PHYSICAL RADIATION EFFECTS; PROTEINS; RADIATION EFFECTS
Optional Information
- Contract/Grant/Project number
- KC0402010; ERKCSNX; AC05-00OR22725
- Notes
- doi 10.1007/s10867-009-9184-6
- Funding organization
- SC USDOE - Office of Science (United States)