green fluorescence protein (gfp)

GFP is a fluorescent protein isolated from coelenterates. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. The gene for GFP has been isolated and has become a useful tool for making chimeric proteins of GFP linked to other proteins where it functions as a fluorescent protein tag. As a noninvasive fluorescent marker in living cells, it allows for a wide range of applications where it may function as a cell lineage tracer, reporter of gene expression, or as a measure of protein-protein interactions.

These pages illustrate aspects of fluorescence spectroscopy that are useful for elucidating structural and dynamic properties of proteins. Fluorescent techniques can provide parameters consistent with crystallographic results. The various environments of the fluorophores of a folded protein and the unique stereochemistry of the polypeptide chain affect the fluorophores in many ways which can be used to characterize and to follow changes in the folded conformation in solution. Fluorescence-based techniques can give information about a protein's conformation, binding sites, solvent interactions, degree of flexibility, internal motions, rotational diffusion coefficient, and many other physicochemical parameters.

Article describing the use of GFP - green fluorescent protein. Includes the discovery and 2008 Nobel prize winners for the use of GFP.