Dynamical Transition of Collective Motions in Dry Proteins

Zhuo Liu; Juan Huang; Madhusudan Tyagi; Hugh O'Neill; Qiu Zhang; Eugene Mamontov; Nitin Jain; Yujie Wang; Jie Zhang; Jeremy C. Smith; Liang Hong

doi:10.1103/PhysRevLett.119.048101

Dynamical Transition of Collective Motions in Dry Proteins

Zhuo Liu, Juan Huang, Madhusudan Tyagi, Hugh O'Neill, Qiu Zhang, Eugene Mamontov, Nitin Jain, Yujie Wang, Jie Zhang, Jeremy C. Smith, Liang Hong

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31 Scopus citations

Abstract

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. 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.

Original language	English
Article number	048101
Journal	Physical Review Letters
Volume	119
Issue number	4
DOIs	https://doi.org/10.1103/PhysRevLett.119.048101
State	Published - Jul 25 2017

Funding

The SJTU group acknowledges support from the Center for High Performance Computing (HPC) facility at Shanghai Jiao Tong University, Thermo Gravimetric Analyzer (TGA) in Instrumental Analysis Center of SJTU, and NSF China 11504231 and 31630002. H. O'N and Q.Z. acknowledge the support of the Center for Structural Molecular Biology (FWP ERKP291) funded by the U.S. Department of Energy (DOE) Office of Biological and Environmental Research. The neutron scattering experiment on BASIS (SNS, ORNL) was supported by the Scientific User Facilities Division, Office of Basic Energy Sciences, U.S. Department of Energy. Oak Ridge National Laboratory is managed by UT-Battelle, LLC, for the U.S. DOE under Contract No.DE-AC05-00OR22725. J.C.S. acknowledges support from the Office of Basic Energy Sciences of the United States Department of Energy via a Laboratory-Directed Research and Development grant. This work utilized facilities supported in part by the National Science Foundation under Agreement No.DMR-1508249.

Funders	Funder number
Center for Structural Molecular Biology	FWP ERKP291
Scientific User Facilities Division
National Science Foundation	31630002, 11504231
U.S. Department of Energy
Basic Energy Sciences
Biological and Environmental Research
Oak Ridge National Laboratory
Laboratory Directed Research and Development
Shanghai Jiao Tong University

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AU - Huang, Juan

AU - Tyagi, Madhusudan

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AU - Mamontov, Eugene

AU - Jain, Nitin

AU - Wang, Yujie

AU - Zhang, Jie

AU - Smith, Jeremy C.

AU - Hong, Liang

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AB - 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. 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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Dynamical Transition of Collective Motions in Dry Proteins

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