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Updated: Jan 25, 2026
11:14
Combining Wet and Dry Lab Techniques to Guide the Crystallization of Large Coiled-coil Containing Proteins
Published on: January 6, 2017
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Structural determinants of coiled coil mechanics
Patricia López-García1, Melis Goktas, Ana E Bergues-Pupo
1Max Planck Institute of Colloids and Interfaces, Mechano(bio)chemistry, Science-Park Potsdam Golm, 14424 Potsdam, Germany. kerstin.blank@mpikg.mpg.de.
Physical Chemistry Chemical Physics : PCCP
|April 25, 2019
Summary
Coiled coils (CCs) are crucial for cell-matrix signaling. Understanding helix propensity and core packing is key to engineering CCs as nanomechanical building blocks for biomaterials and drug delivery.
Area of Science:
- Biophysics
- Materials Science
- Cell Biology
Background:
- Coiled coils (CCs) are abundant in biological structures like the cytoskeleton and extracellular matrix.
- CCs are vital for mechanobiochemical signaling between cells and their environment.
- Their structural simplicity enables applications in protein-origami, drug delivery, and biomaterials.
Purpose of the Study:
- To investigate the influence of helix propensity and hydrophobic core packing on the mechanical stability of CC heterodimers.
- To establish CCs as tunable nanomechanical building blocks.
Main Methods:
- Utilized single-molecule force spectroscopy.
- Analyzed force-induced dissociation in a shear loading geometry.
Main Results:
- Both helix propensity and hydrophobic core packing dictate mechanical stability.
- Decreased helix propensity lowers the energy barrier and reduces the distance to the transition state.
- Less tightly packed hydrophobic cores increase the distance to the transition state, potentially due to side chain dynamics and solvation effects.
Conclusions:
- Helix propensity and hydrophobic core packing have distinct effects on the CC energy landscape.
- These parameters must be carefully considered when designing CCs for specific applications.
- Findings advance the engineering of CCs as functional nanomechanical components.
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