Crystal Structure of the Aequorea victoria Green Fluorescent Protein

@article{Ormo1996CrystalSO,
  title={Crystal Structure of the Aequorea victoria Green Fluorescent Protein},
  author={Mats Ormö and Andrew B. Cubitt and Karen Kallio and Larry A Gross and Roger Tsien and S. James Remington},
  journal={Science},
  year={1996},
  volume={273},
  pages={1392 - 1395}
}
The green fluorescent protein (GFP) from the Pacific Northwest jellyfish Aequorea victoria has generated intense interest as a marker for gene expression and localization of gene products. The chromophore, resulting from the spontaneous cyclization and oxidation of the sequence -Ser65 (or Thr65)-Tyr66-Gly67-, requires the native protein fold for both formation and fluorescence emission. The structure of Thr65 GFP has been determined at 1.9 angstrom resolution. The protein fold consists of an 11… 

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References

SHOWING 1-10 OF 36 REFERENCES

Chemical structure of the hexapeptide chromophore of the Aequorea green-fluorescent protein.

The characterization of the Aequorea victoria GFP chromophore is described, which is released as a hexapeptide upon digestion of the protein with papain, formed upon cyclization of the residues Ser-dehydroTyr-Gly within the polypeptide.

SPECTRAL PERTURBATIONS OF THE AEQUOREA GREEN‐FLUORESCENT PROTEIN

Abstract— In the jellyfish Aequorea, the green‐fluorescent protein (GFP) functions as the in vivo bio‐luminescence emitter via energy transfer from the photoprotein aequorin. Accumulated evidence has

Using GFP to see the light.

  • D. Prasher
  • Biology, Chemistry
    Trends in genetics : TIG
  • 1995

Reversible denaturation of Aequorea green-fluorescent protein: physical separation and characterization of the renatured protein.

The green-fluorescent protein (GFP) that functions as a bioluminescence energy transfer acceptor in the jellyfish Aequorea has been renatured with up to 90% yield following acid, base, or guanidine

Intermolecular energy transfer in the bioluminescent system of Aequorea.

In the present study, GFP has been purified, crystallized, and partially characterized and an energy transfer in citro from aequorin to this protein has been demonstrated.