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High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water
Published on: April 28, 2022
Hydration and temperature interdependence of protein picosecond dynamics
Ferdinand Lipps1, Seth Levy, A G Markelz
1IFW Dresden, Leibniz Institute for Solid State and Materials Research, D-01171 Dresden, Germany. f.lipps@ifw-dresden.de
Physical Chemistry Chemical Physics : PCCP
|April 4, 2012
Summary
Protein dynamical transitions depend on solvent motions. Hydration levels critical for these picosecond dynamics are frequency-dependent, requiring minimal water clusters for some motions and a full network for others.
Area of Science:
- Biophysics
- Protein dynamics
- Solvent effects
Background:
- The protein dynamical transition describes a rapid change in protein motion with temperature around 220 K.
- Understanding the role of solvent (water) in protein dynamics is crucial for biological function.
Purpose of the Study:
- To investigate the solvent motions responsible for the protein dynamical transition.
- To examine how hydration and temperature influence protein picosecond dynamics.
Main Methods:
- Terahertz time domain spectroscopy was used to measure the complex permittivity of myoglobin.
- Measurements were conducted in the 0.2-2.0 THz frequency range.
Main Results:
- Both real and imaginary permittivity parts showed strong temperature dependence at hydration levels >0.27 g water/g protein.
- The permittivity change was most pronounced at frequencies below 1 THz.
- Critical hydration for the dynamical transition varied with frequency (0.19 h for >1 THz, 0.27 h for <1 THz).
Conclusions:
- Solvent fluctuations driving the dynamical transition may only require small water clusters (~5 molecules).
- Enhancement of low-frequency protein motions necessitates a complete water network.
- Protein vibrations appear slaved to solvent excitations, not solely governed by bound water relaxation.
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