
The author explores the decoupling of anharmonicity onset between protein and water dynamics around 200 K, revealing intrinsic transitions in both components.


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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 labelling, we found that the onset of anharmonicity in the two components around 200 K are 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.

### Competing Interest Statement

The authors have declared no competing interest.

Decoupling of the Onset of Anharmonicity between a Protein and Its Surface Water around 200 K

decoupling-of-protein-and-water-dynamics-at-200-k


Decoupling of Protein and Water Dynamics at 200 K
