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Coupling of protein and environment fluctuations
1Center for Biological Physics, Arizona State University, PO Box 871604, Tempe AZ 85287, USA.
Biochimica Et Biophysica Acta
|May 31, 2011
Summary
A unified model explains protein dynamics, heat flow, and spatial fluctuations in myoglobin (Mb) powders. This model connects hydration-shell processes to experimental data, revealing kinetic effects and protein motion slaving.
Area of Science:
- Biophysics
- Protein Dynamics
- Materials Science
Background:
- Protein dynamics are crucial for function.
- Previous models have limitations in explaining complex behaviors.
- Myoglobin (Mb) serves as a model system for studying protein dynamics.
Purpose of the Study:
- To review and extend the unified model of protein dynamics.
- To apply the model to heat flow and spatial fluctuations in hydrated myoglobin powders.
- To explain experimental data using the unified model.
Main Methods:
- Review of protein dynamics concepts over 35 years.
- Application of the unified model to myoglobin (Mb) powders.
- Analysis of differential scanning calorimetry (DSC) and incoherent neutron scattering (INS) data.
- Utilizing dielectric relaxation spectroscopy (DRS) to measure hydration-shell processes.
Main Results:
- The unified model successfully explains DSC and INS data for hydrated Mb powders.
- Temperature dependence of data is attributed to hydration-shell β(h) process and fluctuation rates.
- Model accounts for kinetic effects due to experimental time windows and broad rate distributions.
- Slaving of large-scale protein motions to bulk solvent α process is reviewed.
Conclusions:
- The unified model provides a comprehensive framework for understanding protein dynamics, heat flow, and spatial fluctuations.
- Hydration-shell dynamics play a key role in the macroscopic properties of proteins.
- Metastability of myoglobin molecules in glassy solvents at low temperatures is highlighted.
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