Chemical and Biological Sensing Utilizing Fused Bacteriorhodopsin Protein Hybrids
Abstract
This paper describes how monomeric bR can be overproduced in Escherichia coli and subsequently utilized as an integral component of a generic, nanoscale chemical sensing platform. The utility of this sensing platform is that it can be adapted for detection of a wide range of biological and chemical agents at, or below, nanomolar concentration levels. The gene encoding for bacteriorhodopsin has been successfully isolated from Halobacterium salinarum strain S9P using a colony-level PCR approach. Utilizing this purified DNA and a plasmid expression vector system, a fused protein hybrid consisting of maltose binding protein and bacterio-opsin has been expressed in transformed E. coli. The fusion hybrid has been purified in soluble form from E. coli cell-free extracts at up to 70mg/L. Renaturation studies to incorporate all-trans retinal within the bacterio-opsin protein are currently underway.
Document Details
- Document Type
- Technical Report
- Publication Date
- Dec 01, 2008
- Accession Number
- ADA505792
Entities
People
- Craig R. Friedrich
- Donald R. Lueking
- Eric M. Winder
- Mark H Griep
Organizations
- Michigan Technological University