Intrinsic electronic conductivity of individual atomically resolved amyloid crystals reveals micrometer-long hole hopping via tyrosines
Abstract
The ability to understand and modulate protein conductance is central to many biological processes and for the technological applications of electronic biomaterials. However, measurements of intrinsic protein conductivity are lacking. Here, we employ a four-electrode method to measure contact-free electronic conductivity of an individual protein microcrystal that exhibits efficient hole transport over micrometers via stacked tyrosines. Combined experimental and computational studies show that both the energetics and proximity of the proton acceptor to tyrosine determine the rate of hole transport. Our mechanistic studies on model systems with atomic-resolution structures may help identify design principles to engineer electronic conductivity in proteins of interest for a wide range of applications, including artificial photosynthesis, biocatalysis, prevention of oxidative damage, and nucleic acid biosynthesis.
Document Details
- Document Type
- Pub Defense Publication
- Publication Date
- Dec 28, 2020
- Source ID
- 10.1073/pnas.2014139118
Entities
People
- Calina Glynn
- Catharine Shipps
- David Eisenberg
- David R Boyer
- Dennis Vu
- H. Ray Kelly
- Michael R Sawaya
- Nikhil S. Malvankar
- Peter J. Dahl
- Sophia M Yi
- Victor S Batista
Organizations
- Air Force Office of Scientific Research
- National Institute of Allergy and Infectious Diseases
- National Science Foundation
- University of California
- University of California, Los Angeles
- Yale University