Decoupling of the onset of anharmonicity between a protein and its surface water around 200 K
Year: 2024
Type: article
Abstract: The protein dynamical transition at ~200 K, where the biomolecule transforms from a harmonic, non-functional form to an anharmonic, functional state, has been thought to be slaved to the thermal activation of dynamics in its surface hydration water. Here, by selectively probing the dynamics of protein and hydration water using elastic neutron scattering and isotopic labeling, we found that the onset of anharmonicity in the two components around 200 K is decoupled. The one in protein is an intrinsic transition, whose characteristic temperature is independent of the instrumental resolution time, but varies with the biomolecular structure and the amount of hydration, while the one of water is merely a resolution effect.
Source: eLife
Institutions: Shanghai Jiao Tong University, University of Michigan, Michigan Medicine, National Institute of Standards and Technology, NIST Center for Neutron Research, University of Maryland, College Park, Rutherford Appleton Laboratory, Science and Technology Facilities Council, ISIS Neutron and Muon Source, Comprehensive Research Organization for Science and Society, CROSS Neutron Science and Technology Center, Oak Ridge National Laboratory, Shanghai Artificial Intelligence Laboratory
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: gold
Estimated APC paid: $2,500
OpenAlex ID: W4401698305