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[Equilibrium intramolecular mobility in proteins]
Ukrainskii Biokhimicheskii Zhurnal (1978)
|July 1, 1981
Summary
Protein intramolecular mobility, characterized by distinct fast and slow movements, influences protein function and reaction dynamics. Fast mobility, occurring below 10(-6) seconds, creates dynamic microstates affecting protein interior viscosity and reaction parameters.
Area of Science:
- Biophysics
- Protein Dynamics
- Molecular Mobility
Context:
- Proteins exhibit complex internal motions crucial for their biological functions.
- Understanding these motions requires analyzing their characteristic times, probabilities, and spatial scales.
- Existing data on protein intramolecular mobility is critically analyzed and systematized.
Purpose:
- To differentiate between fast (τ < 10⁻⁶ s) and slow (τ > 10⁻⁶ s) intramolecular mobility in proteins.
- To review methods for investigating fast protein mobility, including X-ray analysis, NMR spectroscopy, and fluorescence techniques.
- To elucidate the characteristics and implications of fast protein mobility.
Summary:
- Fast intramolecular mobility is prevalent in proteins, creating dynamic microstates influenced by local packing and bonding.
- These fast movements are localized, possess low activation energies, and represent a limited diffusion process in a viscous protein interior.
- Fast mobility significantly impacts the protein interior's 'viscosity' and influences the activation parameters for protein reactions.
Impact:
- Fast protein dynamics, while not causing large conformational changes, modulate protein function by affecting the internal environment.
- The distribution of dynamic microstates resulting from fast mobility influences the activation parameters of protein-catalyzed reactions.
- This work provides a framework for understanding how internal protein motion contributes to biological activity.