Dooling, Lawrence and Tirrell, David (2018) Engineering dynamic behavior in protein networks. In: 255th American Chemical Society National Meeting & Exposition, March 18-22, 2018, New Orleans, LA. https://resolver.caltech.edu/CaltechAUTHORS:20180412-154255921
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Abstract
In protein-based materials, the amino acid sequence can encode chem. and biol. activity and macroscopic material properties. Here, we describe two approaches to engineer the dynamic behavior of protein networks that contain coiled-coil phys. cross-links. The first is a protein engineering approach in which we have introduced single point mutations within the coiled-coil domain. Hydrogels prepd. from these protein variants exhibit stress relaxation times that vary from less than 1 s to greater than 1000 s. The second approach to modulate network dynamics uses small hydrophobic ligands that bind within the pore of the coiled coil. Addn. of ligands including fatty acids and vitamin D stabilizes phys. cross- links and slows network relaxation by up to three orders of magnitude. Together, these approaches demonstrate that the dynamic behavior of protein networks is highly sensitive to the mol. details of the phys. cross-links. As a result, network dynamics can be encoded within an amino acid sequence or engineered post- fabrication by formulating protein hydrogels with the appropriate ligands.
Item Type: | Conference or Workshop Item (Paper) | ||||||
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Additional Information: | © 2018 American Chemical Society. | ||||||
Record Number: | CaltechAUTHORS:20180412-154255921 | ||||||
Persistent URL: | https://resolver.caltech.edu/CaltechAUTHORS:20180412-154255921 | ||||||
Usage Policy: | No commercial reproduction, distribution, display or performance rights in this work are provided. | ||||||
ID Code: | 85795 | ||||||
Collection: | CaltechAUTHORS | ||||||
Deposited By: | Tony Diaz | ||||||
Deposited On: | 12 Apr 2018 23:03 | ||||||
Last Modified: | 03 Oct 2019 19:35 |
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