My Protein Paper - Kimberly DeVivo Due Wednesday October 5...

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Kimberly DeVivo Due: Wednesday, October 5, 2011 My Protein Paper: Green Fluorescent Protein (1kys) Green Fluorescent Protein (GFP), first found in jellyfish, Aequorea Victoria, is an 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 Aequorea Victoria 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 Page 1 of 6
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BFPms1 does not have a selenomethionoine group that is used in structure 1ema to obtain phasing information from recombinant protein. BFPms1 is in the fluorescent protein family, alpha and beta (α+β) class, and a GFP-like fold such that it has a distinctive 11-stranded β-barrel fold with an α-helix running in the middle of the cylinder shape of the protein. The 11 β-barrel strands are made from 9-13 residues each. The NH2- terminal half of the polypeptide comprises three antiparallel strands, the central helix, and
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My Protein Paper - Kimberly DeVivo Due Wednesday October 5...

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