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High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States
Published on: June 29, 2021
Self-similar dynamics of proteins under hydrostatic pressure-Computer simulations and experiments
1Centre de Biophysique Moléculaire, 45071 Orléans, France. kneller@cnrs-orleans.fr
Biochimica Et Biophysica Acta
|June 23, 2009
Summary
Protein internal dynamics show self-similar behavior across a vast time range, from nanoseconds to hours. This autosimilarity, explained by fractional Brownian dynamics, aids in interpreting complex experimental and simulation data.
Area of Science:
- Biophysics
- Computational Biology
- Physical Chemistry
Background:
- Proteins exhibit complex internal dynamics crucial for function.
- Experimental and simulation studies reveal autosimilarity in protein dynamics over microseconds to hours.
- This dynamics is also observed on nanosecond timescales, accessible via quasielastic neutron scattering.
Purpose of the Study:
- To introduce the theory of fractional Brownian dynamics.
- To demonstrate its utility in interpreting protein dynamics.
- To apply the model to neutron scattering and molecular dynamics simulations under hydrostatic pressure.
Main Methods:
- Kinetic studies of ligand binding.
- Fluorescence correlation spectroscopy.
- Quasielastic neutron scattering experiments.
- Molecular dynamics simulations.
- Fractional Brownian dynamics modeling.
Main Results:
- Protein internal dynamics display autosimilarity from microseconds to hours.
- This autosimilarity is present on nanosecond timescales.
- Long-time memory effects lead to non-exponential decay in time correlation functions.
- Fractional Brownian dynamics effectively models these dynamics.
Conclusions:
- Fractional Brownian dynamics is a suitable model for internal protein dynamics.
- The model aids in interpreting experimental data (neutron scattering) and simulations (molecular dynamics).
- Understanding protein dynamics under hydrostatic pressure is enhanced by this approach.
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