Journal
PHYSICAL REVIEW LETTERS
Volume 119, Issue 4, Pages -Publisher
AMER PHYSICAL SOC
DOI: 10.1103/PhysRevLett.119.048101
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Funding
- U.S. Department of Energy [DE-AC05-00OR22725]
- United States Government
- Department of Energy
- Center for High Performance Computing (HPC) facility at Shanghai Jiao Tong University
- Thermo Gravimetric Analyzer (TGA) in Instrumental Analysis Center of SJTU
- NSF China [11504231, 31630002]
- Center for Structural Molecular Biology - U.S. Department of Energy (DOE) Office of Biological and Environmental Research [FWP ERKP291]
- Scientific User Facilities Division, Office of Basic Energy Sciences, U.S. Department of Energy
- U.S. DOE [DE-AC05-00OR22725]
- Office of Basic Energy Sciences of the United States Department of Energy via a Laboratory-Directed Research and Development grant
- National Science Foundation [DMR-1508249]
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Water is widely assumed to be essential for protein dynamics and function. In particular, the well-documented dynamical transition at similar to 200 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.
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