Quasielastic neutron scattering in biology: Theory and applications.
Neutrons scatter quasielastically from stochastic, diffusive processes, such as overdamped vibrations, localized diffusion and transitions between energy minima. In biological systems, such as proteins and membranes, these relaxation processes are of considerable physical interest. We review here recent methodological advances and applications of quasielastic neutron scattering (QENS) in biology, concentrating on the role of molecular dynamics simulation in generating data with which neutron profiles can be unambiguously interpreted. We examine the use of massively-parallel computers in calculating scattering functions, and the application of Markov state modeling. The decomposition of MD-derived neutron dynamic susceptibilities is described, and the use of this in combination with NMR spectroscopy. We discuss dynamics at very long times, including approximations to the infinite time mean-square displacement and nonequilibrium aspects of single-protein dynamics. Finally, we examine how neutron scattering and MD can be combined to provide information on lipid nanodomains. This article is part of a Special Issue entitled "Science for Life" Guest Editor: Dr. Austen Angell, Dr. Salvatore Magazù and Dr. Federica Migliardo.
Center for Molecular Biophysics, Oak Ridge National Laboratory, TN 37831, USA; Department of Biochemistry and Cellular and Molecular Biology, University of Tennessee, Knoxville, TN 37996, USA.
Derya
D
Vural
Center for Molecular Biophysics, Oak Ridge National Laboratory, TN 37831, USA; Department of Biochemistry and Cellular and Molecular Biology, University of Tennessee, Knoxville, TN 37996, USA.
Xiaohu
X
Hu
Institute of Natural Sciences & Department of Physics and Astronomy, Shanghai Jiao Tong University, 200240, China.
Benjamin
B
Lindner
Center for Molecular Biophysics, Oak Ridge National Laboratory, TN 37831, USA; Department of Biochemistry and Cellular and Molecular Biology, University of Tennessee, Knoxville, TN 37996, USA.
Nitin
N
Jain
Center for Molecular Biophysics, Oak Ridge National Laboratory, TN 37831, USA; Department of Biochemistry and Cellular and Molecular Biology, University of Tennessee, Knoxville, TN 37996, USA.
Yinglong
Y
Miao
Center for Molecular Biophysics, Oak Ridge National Laboratory, TN 37831, USA; Department of Biochemistry and Cellular and Molecular Biology, University of Tennessee, Knoxville, TN 37996, USA.
Xiaolin
X
Cheng
Institute of Natural Sciences & Department of Physics and Astronomy, Shanghai Jiao Tong University, 200240, China.
Zhuo
Z
Liu
Institute of Natural Sciences & Department of Physics and Astronomy, Shanghai Jiao Tong University, 200240, China.
Liang
L
Hong
Center for Molecular Biophysics, Oak Ridge National Laboratory, TN 37831, USA; Department of Biochemistry and Cellular and Molecular Biology, University of Tennessee, Knoxville, TN 37996, USA. Electronic address: smithjc@ornl.gov.
Jeremy C
JC
Smith
D001695:Biology / Q000379:methods*; D018360:Crystallography, X-Ray; D004548:Elasticity; D006859:Hydrogen / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy; D008390:Markov Chains; D056004:Molecular Dynamics Simulation; D009113:Muramidase / Q000737:chemistry; D033363:Neutron Diffraction / Q000379:methods; D010735:Phosphoglycerate Kinase / Q000737:chemistry; D000072417:Protein Domains; D013113:Spin Labels; D013696:Temperature; D014867:Water / Q000737:chemistry
D013113:Spin Labels; D014867:Water; D006859:Hydrogen; D010735:Phosphoglycerate Kinase; D009113:Muramidase
Biomolecules; Dynamics; MD simulation; Neutron scattering