Published: July 28, 2017
Zhuo Liu, Juan Huang, Madhusudan Tyagi, Hugh O'Neill, Qiu Zhang, Eugene Mamontov, NItin Jain, Yujie Wang, Jie Zhang, Jeremy C. Smith, Liang Hong
Water is widely assumed to be essential for protein dynamics and function. In particular, the well-documented "dynamical" transition at ~200 K detected in hydrogenated proteins by incoherent neutron scattering, at which the protein changes from a rigid, non-functional form to a flexible, functional state, 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 thermal activation of collective heavy-atom motions. The dynamical transition discovered is intrinsic to the energy landscape of dry proteins.
Citation: Physical Review Letters
Pub Type: Journals
Dynamical transition, protein, neutron scattering
Created July 28, 2017, Updated November 03, 2017