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High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water

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Published on: April 28, 2022

Does the dynamic Stokes shift report on slow protein hydration dynamics?

Bertil Halle¹, Lennart Nilsson

¹Biophysical Chemistry, Center for Molecular Protein Science, Lund University, SE-22100 Lund, Sweden. bertil.halle@bpc.lu.se

The Journal of Physical Chemistry. B

|May 26, 2009

Summary

Protein-attached probes show slow fluorescence decay, not due to water motion, but solvent polarization. This suggests fluorescence spectroscopy may not reveal protein hydration dynamics.

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Area of Science:

Biophysics
Physical Chemistry
Spectroscopy

Background:

Time-dependent fluorescence spectroscopy is used to study molecular dynamics.
Protein hydration dynamics are crucial for protein function.
Previous studies attributed slow fluorescence decay in protein probes to water motion.

Purpose of the Study:

To investigate the origin of slow fluorescence frequency shift decay in protein-attached probes.
To challenge the prevailing interpretation of slow water motions.
To propose an alternative explanation based on solvent polarization.

Main Methods:

Time-dependent fluorescence spectroscopy measurements.
Analysis of fluorescence frequency shift decay times.
Theoretical modeling using a dielectric continuum model.

Main Results:

Fluorescence decay times for protein-attached probes are significantly slower than for free probes.
The observed slow decay can be explained by solvent polarization, not slow water motions.
Dielectric continuum model supports the solvent polarization mechanism.

Conclusions:

The long decay times in fluorescence shift spectroscopy do not reflect protein hydration dynamics.
Solvent polarization is a key factor influencing fluorescence decay in protein-bound probes.
Re-evaluation of fluorescence spectroscopy data interpretation is needed for protein hydration studies.