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Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
Published on: July 16, 2017
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Engineering the Dynamic Properties of Protein Networks through Sequence Variation
Lawrence J Dooling1, David A Tirrell1
1Division of Chemistry and Chemical Engineering, California Institute of Technology , 1200 East California Boulevard, Pasadena, California 91125, United States.
ACS Central Science
|December 8, 2016
Summary
Scientists programmed the relaxation behavior of protein-based hydrogels by altering their genetic sequences. Subtle genetic changes shifted material relaxation times over five orders of magnitude, enabling control over soft material mechanics.
Area of Science:
- Materials Science
- Biotechnology
- Polymer Chemistry
Background:
- Macromolecular network dynamics govern soft material mechanical properties.
- In protein hydrogels, transient physical junctions dictate stress relaxation and energy dissipation.
Purpose of the Study:
- To demonstrate programming of relaxation behavior in engineered protein networks.
- To investigate the impact of sequence modifications on material dynamics.
Main Methods:
- Engineered coiled-coil proteins were used to create end-linked networks.
- Dynamic oscillatory shear rheometry and stress relaxation measurements were employed.
- Single-site substitutions within coiled-coil domains were systematically introduced.
Main Results:
- Subtle sequence changes resulted in shifts of relaxation time spanning five orders of magnitude.
- The ability to engineer networks with multiple relaxation time scales was demonstrated.
- Genetic sequence directly correlates with time-dependent mechanical responses.
Conclusions:
- Genetic information can be used to encode the time-dependent mechanical properties of macromolecular materials.
- This approach offers precise control over the dynamic behavior of protein-based soft materials.
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