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Updated: Jul 10, 2026
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High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States
Published on: June 29, 2021
Picosecond fluctuating protein energy landscape mapped by pressure temperature molecular dynamics simulation
Lars Meinhold1, Jeremy C Smith, Akio Kitao
1Physical Biology Center for Ultrafast Science and Technology, California Institute of Technology, 1200 East California Boulevard M/C 127-72, Pasadena, CA 91125, USA.
Summary
Pressure significantly affects protein vibrations and energy dissipation, but not the overall energy landscape barriers. This suggests a dynamic, fluctuating view of protein energy landscapes is crucial for understanding relaxation processes.
Area of Science:
- Biophysics
- Computational Biology
- Protein Dynamics
Background:
- Protein energy landscapes govern protein function and dynamics.
- Microscopic pressure fluctuations can theoretically influence protein shape and energy landscapes.
Purpose of the Study:
- To investigate the impact of pressure on protein energy landscapes.
- To understand how pressure affects protein conformational substates and dynamics.
Main Methods:
- Nanosecond molecular dynamics simulations of lysozyme.
- Simulations conducted across a range of temperatures and pressures.
Main Results:
- The dynamical transition with temperature is pressure-independent.
- Vibrations within protein substates stiffen with increasing pressure.
- Pressure increases damping of low-frequency collective modes, enhancing energy dissipation.
Conclusions:
- Protein energy landscapes are better described by a fluctuating model than an invariant one.
- Pressure-dependent energy dissipation mechanisms are critical for protein function and relaxation.
