Thermal characterization and differential scanning calorimetric investigations of wild type green and blue proteorhodopsins

BIOL 102

Matthew J. Ranaghan, mjr03009@gmail.com1, Gregg Whited2, Arlene D. Albert1, and Robert R. Birge3. (1) Department of Molecular and Cell Biology, University of Connecticut, 91 North Eagleville Road, Storrs, CT 06269, (2) Silicon Biotechnology program, Genecor International Inc, 925 Page Mill Road, Palo Alto, CA94304, (3) Department of Chemistry, University of Connecticut, 55 North Eagleville Rd., Storrs, CT 06269
Proteorhodopsin (PR) is a newly characterized type I rhodopsin identified in an uncultivated marine bacterium and is the first of its kind reported in eubacteria. This protein has also generated significant interest as a replacement for bacteriorhodopsin in photonic devices. This interest is due in part to a similar photocycle, good stability and the ability to grow large quantities using efficient and inexpensive bacterial hosts. However, little is known about the structure-function relationships in PR nor the origins of its remarkable stability. Differential scanning calorimetry (DSC) and isothermal denaturation kinetic traces give insight to the conformational state of PR by characterization of the thermal parameters of the molecule. Our studies provide strong evidence that PR molecules are associated in solution and analysis of the data suggests a trimeric quaternary structure.
 

Frontiers in Chemical Biology
5:00 PM-7:00 PM, Sunday, August 19, 2007 BCEC -- Exhibit Hall - B2, Poster

Division of Biological Chemistry

The 234th ACS National Meeting, Boston, MA, August 19-23, 2007