Reveal protein dynamics by combining computer simulation and neutron scattering

Protein carries out most functions in living things on the earth through characteristic modulation of its three-dimensional structure over time. Understanding the microscopic nature of the protein internal motion and its connection to the function and structure of the biomolecule is a central topic in biophysics, and of great practical importance for drug design, study of diseases, and the development of renewable energy, etc. Under physiological conditions, protein exhibits a complex dynamics landscape, i.e., a variety of diffusive and conformational motions occur on similar time and length scales. This variety renders difficult the derivation of a simplified description of protein internal motions in terms of a small number of distinct, additive components. This difficulty is overcome by our work using a combined approach of Molecular Dynamics (MD) simulations and the Neutron Scattering experiments [1]. Our approach enables distinct protein motions to be characterized separately, furnishing an in-depth understanding of the connection between protein structure, dynamics and function [2,3]. \\[4pt] [1] L. Hong, \textit{et al.}, Phys. Rev. Lett. 107 (2011) 148102. \\[0pt] [2] L. Hong, \textit{et al.}, Phys. Rev. Lett. 108 (2012) 238102. \\[0pt] [3] L. Hong, \textit{et al.}, Phys. Rev. Lett. 110 (2013) 028104.