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High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water
Published on: April 28, 2022
Depth dependent dynamics in the hydration shell of a protein
J Servantie1, C Atilgan, A R Atilgan
1Faculty of Engineering and Natural Sciences, Sabanci University, Orhanli 34956 Tuzla, Istanbul 34956, Turkey. cservantie@sabanciuniv.edu
The Journal of Chemical Physics
|September 7, 2010
Summary
Hydration water dynamics influence protein flexibility. Below a transition temperature, water acts as a rigid crust, but upon transition, it unfreezes, enhancing protein atomic fluctuations and flexibility.
Area of Science:
- Biophysics
- Computational Biology
- Protein Dynamics
Background:
- Protein function is intrinsically linked to its dynamic behavior.
- The role of hydration water in modulating protein dynamics is crucial but not fully understood.
Purpose of the Study:
- To investigate the dynamics of water-protein interactions in folded proteins.
- To elucidate the mechanisms behind the dynamical transition in proteins.
- To understand how hydration shell dynamics affect protein flexibility.
Main Methods:
- Utilizing extensive molecular dynamics simulations.
- Analyzing hydration water molecule association with protein residues.
- Tracking water molecule residence times and orientational memory.
Main Results:
- Water molecule association scales linearly with protein depth, independent of backbone dynamics.
- Water residence time inversely scales with depth at physiological temperatures.
- Below the transition, water forms a glassy layer inhibiting protein fluctuations; above it, the hydration shell unfreezes, increasing protein flexibility.
Conclusions:
- Hydration water plays a critical role in protein's dynamical transition.
- The state of the hydration shell directly impacts protein conformational flexibility.
- Understanding these dynamics is key to comprehending protein function.
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