Format

Send to

Choose Destination
Biochem Biophys Res Commun. 2000 Feb 16;268(2):462-5.

Engineered metal binding sites on green fluorescence protein.

Author information

1
Joint Science Department, Claremont McKenna, Pitzer, and Scripps Colleges, 925 North Mills Avenue, Claremont, California 91711, USA. richmond@jsd.claremont.edu

Abstract

The ability to assay a variety of metals by noninvasive methods has applications in both biomedical and environmental research. Green fluorescent protein (GFP) is a protein isolated from coelenterates that exhibits spontaneous fluorescence. GFP does not require any exogenous cofactors for fluorescence, and can be easily appended to other proteins at the DNA level, producing a fluorescence-labeled target protein in vivo. Metals in close proximity to chromophores are known to quench fluorescence in a distance-dependent fashion. Potential metal binding sites on the surface of GFP have been identified and mutant proteins have been designed, created, and characterized. These metal-binding mutants of GFP exhibit fluorescence quenching at lower transition metal ion concentrations than those of the wild-type protein. These GFP mutants represent a new class of protein-based metal sensors.

PMID:
10679227
DOI:
10.1006/bbrc.1999.1244
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center