Use this colorful, 3-D protein model to explain the
structure and function of the green fluorescent protein (GFP), an
example of a beta barrel, and how GFP has become a valuable tool in
Green fluorescent protein (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
three 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.