Due: Wednesday, October 5, 2011
My Protein Paper: Green Fluorescent Protein (1kys)
Green Fluorescent Protein (GFP), first found in jellyfish,
important scientific contribution made by Martin Chalfie, Ph.D., of Columbia University, Roger
Y. Tsien, Ph.D., of the University of California at San Diego, and Osamu Shimomura, Ph.D., of
the Marine Biology Laboratory in Woods Hole, MA. The contributions made by these
individuals was recognized when they accepting the Nobel Prize in chemistry in 2008. Since the
discovery of GFP in
other species such as Renilla reniformis, a sea pansy,
have been found to carry a similar protein to GFP.
Also, there are various mutants’ forms of
fluorescent proteins that have been created to be utilized for many different purposes. One such
structure of GFP mutation (BFPms1), with a PDB reference number of 1kys, is used as a
biosensor for Zinc (Zn) or Cu(II). This structure has a molecular weight of 26973.72 and
contains 239 residues. This particular structure was deposited in 2002-02-05 into the PDB and
was determined by X-ray diffraction with a resolution of 1.44Å.
BFPms1 is a mutant designed by chemists from the original GFP structure found in
nature, PDB reference number 1ema. Both of these structures have an interesting amino acid
composition. The basic structure, 1ema, is made from parent amino acid residue Gly and Try.
One of the significant differences in the 1kys structure is that its parent residue is Gly, Thr, and
His. In the 1kys structure His was incorporated into the structure instead of Tyr group. This can
be seen in figure one. This replacement thus causes the metal ion, Zn, to bind tridentate to the
chromophore, to the side-chain of Glu222, and to a water molecule. Another fascinating fact is
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