Dynamical Transition of Collective Motions in Dry Proteins

Published

July 28, 2017

Author(s)

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

Abstract

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

Volume

119

Issue

4

Pub Type

Journals

Download Paper

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Keywords

Dynamical transition, protein, neutron scattering

Citation

Liu, Z. , Huang, J. , Tyagi, M. , O'Neill, H. , Zhang, Q. , Mamontov, E. , Jain, N. , Wang, Y. , Zhang, J. , Smith, J. and Hong, L. (2017), Dynamical Transition of Collective Motions in Dry Proteins, Physical Review Letters, [online], https://tsapps.nist.gov/publication/get_pdf.cfm?pub_id=923488 (Accessed December 2, 2024)