What Is Green Fluorescent Protein?

Green fluorescent protein ( GFP ) is a protein composed of about 238 amino acids, which can be excited from blue light to ultraviolet light to emit green fluorescent light. Although many other marine organisms have similar green fluorescent proteins, traditionally, green fluorescent protein (GFP) refers to a protein that was first isolated from Victorian multitubular luminescent jellyfish. This protein was first discovered by Shimomura and others in Victoria in multitubular luminous jellyfish in 1962. This light-emitting process also needs the help of the cold-light protein jellyfish, and this cold-light protein can interact with calcium ions.

Green fluorescent protein ( GFP )

In 1962, there have been reports in the literature that scientists have extracted proteins with bioluminescent properties from luminous hydromedusan Aequorea of the genus Jellyfish. Only in the 1970s did some new advances in the phenomenon of bioluminescence. Scientists have studied the intramolecular energy transfer of the multi-tube jellyfish bioluminescence system. Only in the early 1990s did scientists clone the GFP cDNA and study its expressed amino acid sequence, and found that the gfp 10 cDNA encodes 238 amino acid peptides. Studying A. victoria GFP gene clone, it was found that there are three restriction sites on the GFP gene. This will help subsequent scientists to understand its structure.

In February 1994, M. Chalfie and others creatively expressed GFP in Escherichia coli and Caenorhabditis elegans cells, respectively, and concluded that because GFP does not require other substrates or co-acting factors, GFP expression can be used to Monitor gene expression and protein localization in vivo. For a period of time since then, countless researchers have invested in GFP-related research. Just about a month after M. Chalfie reported, Tsuji et al. Fused and expressed the GFP protein in E. coli , and the excitation and emission spectra of GFP in the organism were not significantly different from those under natural conditions. Because the fluorescence intensity of GFP in the organism is not strong enough, it is difficult to apply it to practical scientific research. In 1995, Tsien et al. Increased the fluorescence intensity of GFP, which greatly promoted the application of GFP in biological research. Then in August 1996, F. Yang et al. Analyzed the molecular structure of GFP. The GFP protein is barrel-shaped, with 11 -sheets forming the outer periphery, which has an -helix. Some irregular curls. In September of the same year, Tsien et al. Analyzed the crystal structure of GFP and clarified its principle of light emission. Some scientists also screen for better GFP by making mutants, such as pH-sensitive GFP, GFP specifically for plant cell research, and so on. In addition to optimizing GFP, many scientists have developed ideas and extended the application of GFP protein to many research fields. In 2002, David A. Zacharias et al. Applied GFP protein to the study of membrane proteins. In the same year, the GFP protein was even made into a Zn biodetector.

Wild-type green fluorescent protein, initially a 238 amino acid peptide chain, is about 25 KDa. Then according to certain rules, 11

Since fluorescent proteins can be inherited stably in offspring and can be specifically expressed according to promoters, traditional chemical dyes are slowly replaced in quantitative or other experiments. More, fluorescent proteins have been transformed into different new tools, which not only provide new ideas for solving problems, but also may bring more valuable new problems.

• Molecular and Cell Biology Topics

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