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Study of Protein Dynamics via Neutron Spin Echo Spectroscopy
Published on: April 13, 2022
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Energy propagation and network energetic coupling in proteins.
Andre A S T Ribeiro1, Vanessa Ortiz
1Department of Chemical Engineering, Columbia University , New York, New York 10027, United States.
The Journal of Physical Chemistry. B
|January 9, 2015
Summary
This study introduces energetic coupling to quantify allosteric protein responses by analyzing energy networks. This method effectively identifies active mutants and suggests energy propagation through protein backbones explains signal transmission in disordered proteins.
Area of Science:
- Biophysics
- Structural Biology
- Computational Biology
Background:
- Allosteric proteins are crucial for biological regulation.
- Understanding their environmental response is a key research area.
- Current methods often rely on atomic motion correlations.
Purpose of the Study:
- To introduce a new method for quantifying allosteric protein responses.
- To define and validate 'energetic coupling' as a measure of allosteric activity.
- To explore energy propagation as a mechanism for allosteric signal transmission.
Main Methods:
- Analysis of protein energy networks.
- Development and application of the 'energetic coupling' metric.
- Energy-propagation simulations on various proteins (LacI, CAP, PSD-95).
Main Results:
- Energetic coupling successfully discriminated allosterically active mutants of lactose repressor (LacI) and catabolite activator protein (CAP).
- Energy-propagation simulations validated the assumption that efficient energy propagation, not just atomic motion, underlies allostery.
- Simulations on postsynaptic density protein 95 (PSD-95) indicated the protein backbone is a superior pathway for energy transfer compared to other contacts.
Conclusions:
- Energetic coupling is a viable quantitative measure for allosteric activity.
- Allosteric signal transmission is accurately described by efficient energy propagation.
- Protein backbone energy transfer offers a potential explanation for signal transmission in intrinsically disordered proteins.
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