The green fluorescent protein.

  title={The green fluorescent protein.},
  author={Roger Tsien},
  journal={Annual review of biochemistry},
  • R. Tsien
  • Published 1 July 1998
  • Biology
  • Annual review of biochemistry
In just three years, the green fluorescent protein (GFP) from the jellyfish Aequorea victoria has vaulted from obscurity to become one of the most widely studied and exploited proteins in biochemistry and cell biology. Its amazing ability to generate a highly visible, efficiently emitting internal fluorophore is both intrinsically fascinating and tremendously valuable. High-resolution crystal structures of GFP offer unprecedented opportunities to understand and manipulate the relation between… 

Studying the Green Fluorescent Protein with Single-Molecule Spectroscopy

GFP is the only genetically encodeable protein that fluoresces without the addition of external cofactors and can be expressed in many eukaryotic and prokaryotic cells, making it an ideal marker for highly selective fluorescence labeling of live cells.

Mechanisms of protein fluorophore formation and engineering.

Photoactivation in green to red converting EosFP and other fluorescent proteins from the GFP family

This review aims to give an overview of photoactivatable marker proteins, focusing on the molecular basis of light-induced green to red photoconversion in EosFP.

Green Fluorescent Protein and its Uses

Recognized increased opportunities to understand the relation between GFP structure and its spectroscopic function become available because of the higher resolution of its structure.

Photophysics and high-resolution spectroscopy of green fluorescent protein

The green fluorescent protein (GFP) has recently attracted great attention because it is the only cloned protein that exhibits strong fluorescence without any extraneous chromophores [1]. When fused

Focus on Fluorescent Proteins

Structure–Function Relationships in Fluorescent Marker Proteins of the Green Fluorescent Protein Family

This chapter summarizes the present knowledge of the structural diversity of GFP-like proteins and discusses how structure and dynamics govern their optical properties.

Evolutions in Science Triggered by Green Fluorescent Protein (GFP)

Many efforts were undertaken to optimize this protein by point mutations, which finally led to the generation of a considerably improved GFP, with faster generation of the fluorophore, brighter fluorescence, correct folding at 37 8C, and a single excitation peak at 488 nm.



Fluorescent proteins from nonbioluminescent Anthozoa species

We have cloned six fluorescent proteins homologous to the green fluorescent protein (GFP) from Aequorea victoria. Two of these have spectral characteristics dramatically different from GFP, emitting

Crystal Structure of the Aequorea victoria Green Fluorescent Protein

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


  • M. Chalfie
  • Biology
    Photochemistry and photobiology
  • 1995
This demonstration indicated that GFP could be used as a marker of gene expression and protein localization in living and fixed tissues and variations with more intense fluorescence or alterations in the excitation and emission spectra have been produced.

Structure and dynamics of green fluorescent protein.

  • G. Phillips
  • Biology, Chemistry
    Current opinion in structural biology
  • 1997

Thermosensitivity of green fluorescent protein fluorescence utilized to reveal novel nuclear-like compartments in a mutant nucleoporin NSP1.

Proteins synthesized at a low temperature retained their fluorescence despite a shift to a higher temperature, and when a temperature-sensitive nsp1 mutant expressing GFP-nucleoplasmin was cultured at 23 degrees C and then shifted to 35 degrees C, this protein accumulated in novel nuclear-like compartments devoid of DNA.

Red-Shifted Excitation Mutants of the Green Fluorescent Protein

Using optimized combinatorial mutagenisis techniques and digital imaging Spectroscopy (DIS), we have insulated mutants of the cloned Aequorea victoria green fluorescent protein (GFP)that show

Wavelength mutations and posttranslational autoxidation of green fluorescent protein.

  • R. HeimD. PrasherR. Tsien
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 1994
The availability of two visibly distinct colors should significantly extend the usefulness of GFP in molecular and cell biology by enabling in vivo visualization of differential gene expression and protein localization and measurement of protein association by fluorescence resonance energy transfer.

Green fluorescent protein as a marker in transgenic mice

Green fluorescence was observed in muscle, pancreas, kidney, heart and other organs in all the three transgenic mouse lines and it was demonstrated that the GFP expression could be quantified by measuring the fluorescence in tissue extracts.