GFP is responsible for the green bioluminescence of many marine organisms, including Pacific Northwest jellyfish. Scientists can fuse GFP with proteins from other organisms such as mice or zebra fish, to introduce fluorescence and trace the intra-cellular location of the target protein.

This 3-D model illustrates how GFP’s structure consists of an 11-stranded beta barrel surrounding a central alpha helix containing the fluorophore that emits light. It can be used to discuss secondary structure of proteins, the differences between parallel and anti-parallel beta sheets, and the use of genes and proteins in biotechnology. This alpha carbon backbone mini model is multi-colored to help your students trace the path of the chain from the yellow tip of the N-terminus to the red tip at the C-terminus. They will see that 3 yellow beta strands change to green as the chain moves through the center of the barrel emerging into purple at the other end. From there they will follow the beta strands to cyan and finally red. The fluorophore is located on the green strand at the center of the beta barrel and is shown in a spacefill format.

The 2008 Nobel Prize in Chemistry was awarded jointly to Osamu Shimomura, Martin Chalfie and Roger Y. Tsien "for the discovery and development of the green fluorescent protein, GFP".

This 3'' model is made of plaster by rapid prototyping and should be handled with care. Mini models will break if dropped, held tightly or handled roughly. Its PDB file is 1EMB.pdb.