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Protein Dynamics in Living Cells

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Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments

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Functional-State Dependence of Picosecond Protein Dynamics.

D K George¹, J Y Chen¹, Yunfen He¹

¹Department of Physics, University at Buffalo, SUNY, Buffalo, New York 14260, United States.

The Journal of Physical Chemistry. B

|October 4, 2021

Summary

This summary is machine-generated.

Protein dynamics reveal distinct temperature-dependent behaviors. A lower-energy process linked to collective motions disappears upon denaturing or ligand binding, highlighting structural flexibility in proteins like lysozyme and cytochrome c.

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Area of Science:

Biophysics
Protein Dynamics
Terahertz Spectroscopy

Background:

Proteins exhibit complex dynamics crucial for function.
Understanding these dynamics requires sensitive measurement techniques.
Temperature significantly influences protein conformational changes.

Purpose of the Study:

To investigate temperature-dependent picosecond dynamics of lysozyme and cytochrome c.
To elucidate the nature of protein structural motions and their environmental dependencies.
To correlate observed dynamics with protein structural integrity and ligand interactions.

Main Methods:

Temperature-dependent terahertz permittivity measurements were employed.
Analysis utilized a double Arrhenius model to fit the data.
Comparison between folded, denatured, and ligand-bound protein states.

Main Results:

A double Arrhenius temperature dependence was observed for folded proteins.
Two distinct activation energies (E1 ≈ 0.1 kJ/mol, E2 ≈ 10 kJ/mol) were identified.
The lower activation energy process, linked to correlated structural motions, was absent in denatured proteins and diminished with ligand binding.

Conclusions:

The higher activation energy corresponds to the protein dynamical transition at the solvent-protein interface.
The lower activation energy is attributed to collective structural motions sensitive to protein structure and ligand binding.
These findings suggest that collective motions are essential for protein flexibility and are modulated by structural integrity and ligand interactions.