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Updated: May 16, 2026
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High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States
Published on: June 29, 2021
Unlocking internal prestress from protein nanoshells.
W S Klug1, W H Roos, G J L Wuite
1Department of Mechanical and Aerospace Engineering, and California NanoSystems Institute, UCLA, Los Angeles, California 90095, USA.
Physical Review Letters
|December 11, 2012
Summary
Viral capsids possess internal compressive prestress due to protein assembly geometry. Experiments on herpes simplex virus capsids confirm this internal stress, demonstrating its role in viral structure.
Area of Science:
- Structural biology
- Biophysics
- Virology
Background:
- Icosahedral virus capsids are protein shells with specific geometric arrangements.
- Elasticity theory suggests these structures may contain internal compressive prestress.
- This prestress could explain relationships between capsid size and shape.
Purpose of the Study:
- To experimentally investigate residual prestress in macromolecular assemblies.
- To test the hypothesis that geometric incompatibility of subunits causes prestress.
- To directly measure the mechanical response of virus capsids to subunit removal.
Main Methods:
- Utilized a combination of experimental techniques and elasticity theory.
- Focused on "whiffle ball" capsids of herpes simplex virus.
- Performed controlled removal of protein pentamers from icosahedral vertices.
Main Results:
- Demonstrated the signature of internal prestress in wild-type capsids.
- Provided the first direct experimental evidence for prestress in viral capsids.
- Quantified the mechanical response following pentamer removal.
Conclusions:
- Confirms the presence of internal compressive prestress in icosahedral viral capsids.
- Supports the role of geometric incompatibility in generating this prestress during assembly.
- Establishes a foundation for understanding the mechanics of viral structures.
