Green Fluorescent
Protein (GFP)

Green Fluorescent Protein (GFP)

Green Fluorescent Protein (GFP)

Green Fluorescent Protein (GFP)

Green Fluorescent Protein (GFP) is a bioluminescent protein that was originally isolated from the jellyfish Aequorea victoria. It exhibits bright green fluorescence when exposed to light in the blue to ultraviolet range. GFP has become an invaluable tool in molecular biology, biochemistry, and cell biology due to its ability to act as a biological marker.

Jelly fish

The protein consists of 238 amino acids and forms a barrel-shaped structure, with the fluorescent chromophore located in the center. This chromophore is formed in a unique autocatalytic reaction during protein folding. GFP does not require any additional substrates or cofactors (other than oxygen) to fluoresce, making it an ideal marker for various biological processes.

GFP and its derivatives have been engineered to emit different colors, allowing for the simultaneous visualization of multiple biological processes or molecules within the same cell. These variants have expanded the fluorescent toolkit, enabling researchers to tag proteins, monitor gene expression, track cellular components in real time, and visualize the activity of enzymes.

The discovery and development of GFP as a biological tool were so impactful that the 2008 Nobel Prize in Chemistry was awarded to Osamu Shimomura, Martin Chalfie, and Roger Y. Tsien for their work related to GFP. Shimomura identified and isolated the protein, Chalfie expressed it in other organisms as a fluorescent tag, and Tsien developed the color variants.

GFP’s use in research has revolutionized the way scientists study biological processes at the molecular and cellular levels. It allows for non-invasive observation and provides a powerful means to study the dynamic processes within living cells in real time.

 
Jelly fish

The protein consists of 238 amino acids and forms a barrel-shaped structure, with the fluorescent chromophore located in the center. This chromophore is formed in a unique autocatalytic reaction during protein folding. GFP does not require any additional substrates or cofactors (other than oxygen) to fluoresce, making it an ideal marker for various biological processes.

GFP and its derivatives have been engineered to emit different colors, allowing for the simultaneous visualization of multiple biological processes or molecules within the same cell. These variants have expanded the fluorescent toolkit, enabling researchers to tag proteins, monitor gene expression, track cellular components in real time, and visualize the activity of enzymes.

The discovery and development of GFP as a biological tool were so impactful that the 2008 Nobel Prize in Chemistry was awarded to Osamu Shimomura, Martin Chalfie, and Roger Y. Tsien for their work related to GFP. Shimomura identified and isolated the protein, Chalfie expressed it in other organisms as a fluorescent tag, and Tsien developed the color variants.

GFP’s use in research has revolutionized the way scientists study biological processes at the molecular and cellular levels. It allows for non-invasive observation and provides a powerful means to study the dynamic processes within living cells in real time.

 

References

  • Yang, Fan, Larry G. Moss, and George N. Phillips Jr. The molecular structure of green fluorescent protein. Nature biotechnology 14.10 (1996): 1246-1251.
  • Gadge, S., J. K. Philip, and K. Volmostree. The molecular structure of green fluorescent protein. Journal of Soils and Crops. 25.1 (2015): 13-20.
 

Disclaimer:

No AI or bots were harmed in the creation of this content. AI was used as a tool to supplement and enhance the text, as well as provide suggestions.

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