News & Events

The bacteriorhodopsin carboxyl-terminus influence on protein
Seton Hall > News & Events 

Friday, January 30, 2009
by: Miriam Lyons-Frolow, M.P.A.

George Turner, Ph.D., assistant professor of Chemistry and Biochemistry, and colleagues performed a study entitled “The bacteriorhodopsin carboxyl-terminus contributes to proton recruitment and protein stability”. 
 
The study examined functional and structural roles for the tail end of the membrane protein (and light-receptor) bacteriorhodopsin (bR).  The amino acids comprising the bR tail were removed by recombinant DNA technology. Deletion of the tail had no effect on the inactive form of the membrane protein. Removal of the distal end of the tail had no effect on light-activated photosynthetic mechanism, however, removal of the entire tail severely distorted light-activation. Furthermore, removal of the amino acid tail caused the entire protein to unfold (denature) when exposed to elevated temperatures and the detergent SDS.
 
Taken together the results of this study suggest that this light-receptor protein exhibits two “domains” of stability: 1) a core amino acid domain that surrounds the light-absorbing chromophore; this domain does not know whether the tail is present or not, and 2) the surrounding amino acid bundle whose contributions to protein stability and light-activated function are influenced by long-range interactions with protein tail.
 
This study is being published in Biochemistry and can be found at http://pubs.acs.org. The journal Biochemistry is the leading journal in the fields of Biochemistry and Biophysics and possesses an impact factor of 3.368.

For more information please contact:
Professor George Turner, Department Chemistry and Biochemistry
(973) 761 9598
turnerge@shu.edu