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Dynamical Transition of Collective Motions in Dry Proteins
- Source :
- Physical Review Letters. 119
- Publication Year :
- 2017
- Publisher :
- American Physical Society (APS), 2017.
-
Abstract
- Water is widely assumed to be essential for protein dynamics and function. In particular, the well-documented ``dynamical'' transition at $\ensuremath{\sim}200\text{ }\text{ }\mathrm{K}$, at which the protein changes from a rigid, nonfunctional form to a flexible, functional state, as detected in hydrogenated protein by incoherent neutron scattering, requires hydration. Here, we report on coherent neutron scattering experiments on perdeuterated proteins and reveal that a transition occurs in dry proteins at the same temperature resulting primarily from the collective heavy-atom motions. The dynamical transition discovered is intrinsic to the energy landscape of dry proteins.
- Subjects :
- Neutrons
Physics
Quantitative Biology::Biomolecules
Quantitative Biology::Molecular Networks
Protein dynamics
Temperature
Proteins
Water
General Physics and Astronomy
Energy landscape
State (functional analysis)
Function (mathematics)
Molecular Dynamics Simulation
Neutron scattering
010402 general chemistry
01 natural sciences
0104 chemical sciences
Quantitative Biology::Subcellular Processes
Motion
0103 physical sciences
Atomic physics
010306 general physics
Subjects
Details
- ISSN :
- 10797114 and 00319007
- Volume :
- 119
- Database :
- OpenAIRE
- Journal :
- Physical Review Letters
- Accession number :
- edsair.doi.dedup.....787a099294e5c5254ade82b20c8b1727