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This content will become publicly available on July 25, 2018

Title: Dynamical Transition of Collective Motions in Dry Proteins

Water is widely assumed to be essential for protein dynamics and function. In particular, the well-documented “dynamical” transition at ~ 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. 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. Furthermore, the dynamical transition discovered is intrinsic to the energy landscape of dry proteins.
Authors:
 [1] ;  [1] ;  [2] ;  [3] ;  [3] ;  [4] ;  [5] ;  [1] ;  [1] ;  [6] ;  [1]
  1. Shanghai Jiao Tong Univ. (China)
  2. National Inst. of Standards and Technology (NIST), Shanghai (China)
  3. Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
  4. Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). Spallation Neutron Source (SNS)
  5. Univ. of Tennessee, Knoxville, TN (United States)
  6. Univ. of Tennessee, Knoxville, TN (United States); Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
Publication Date:
Grant/Contract Number:
AC05-00OR22725; DMR-1508249
Type:
Accepted Manuscript
Journal Name:
Physical Review Letters
Additional Journal Information:
Journal Volume: 119; Journal Issue: 4; Journal ID: ISSN 0031-9007
Publisher:
American Physical Society (APS)
Research Org:
Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
Sponsoring Org:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES
OSTI Identifier:
1376609
Alternate Identifier(s):
OSTI ID: 1372727