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Related Experiment Video

Updated: Jun 13, 2026

High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States

High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States

Published on: June 29, 2021

Protein stability at negative pressure.

Edgar Larios¹, Martin Gruebele

¹Department of Physics, University of Illinois at Urbana-Champaign, IL 61801, USA.

Methods (San Diego, Calif.)

|May 4, 2010

Summary

This summary is machine-generated.

Negative pressure destabilizes proteins like ubiquitin, according to NMR and simulations. Further research suggests a potential

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Area of Science:

Protein dynamics and biophysics
Chemical physics of macromolecules

Background:

Protein stability is crucial for biological function.
Understanding pressure effects on protein folding is key to molecular biology.

Purpose of the Study:

To investigate the impact of negative pressure on protein stability.
To explore the relationship between pressure, temperature, and protein free energy.
To identify potential 'islands of stability' for proteins under extreme conditions.

Main Methods:

Proton Nuclear Magnetic Resonance (NMR) spectroscopy at atmospheric and negative pressures.
Molecular dynamics simulations under negative pressure conditions.
Analysis of histidine aromatic resonance in ubiquitin.

Main Results:

Negative pressure was found to destabilize the protein ubiquitin.
Experimental results align with a quadratic free energy dependence on pressure and temperature.
Molecular dynamics simulations confirmed experimental findings and predicted a folding free energy turnaround at very low pressures.

Conclusions:

Negative pressure destabilizes ubiquitin, supporting existing thermodynamic models.
A potential 'island of stability' for proteins may exist at very negative pressures.
Protein folding may occur within low-density solvent fluctuations under extreme negative pressure conditions.