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Time-Resolved Fluorescence Anisotropy from Single Molecules for Characterizing Local Flexibility in Biomolecules
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Correlated Evolution of Low-Frequency Vibrations and Function in Enzymes
Tushar Modi1, Paul Campitelli1, Matthias Heyden2
1Department of Physics, Arizona State University, Tempe, Arizona85287, United States.
The Journal of Physical Chemistry. B
|January 12, 2023
Summary
Protein evolution involves changes in collective vibrational modes. Analyzing these thermal vibrations reveals how protein dynamics drive functional adaptation and the evolution of enzyme properties.
Area of Science:
- Biophysics
- Protein Dynamics
- Evolutionary Biology
Background:
- Protein function evolves through alterations in their native state ensemble.
- Protein flexibility changes are linked to functional evolution.
Purpose of the Study:
- To propose a direct method for analyzing protein evolution by examining thermally activated vibrations.
- To investigate changes in collective protein modes during evolution.
Main Methods:
- Analysis of the backbone vibrational density of states.
- Comparison of vibrational spectra of ancestral and extant proteins (β-lactamases and thioredoxins) below 6 THz.
Main Results:
- Significant changes in the vibrational spectrum were observed in response to protein evolution.
- Shifts in vibrational mode densities correlate with changes in protein flexibility.
Conclusions:
- Protein dynamics and dynamical allostery are crucial for the evolution of enzymes.
- Thermally activated vibrations below 6 THz offer insights into enzyme evolution and adaptation.
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