Green Fluorescent Protein

1. Structure and Application: Green Fluorescent Protein Green fluorescent protein (Green fluorescent protein, GFP), is a composed of about 238 amino acid protein, can make its excitation from blue to ultraviolet ray, a Green fluorescence.While many other Marine organisms have similar GFP proteins, traditionally GFP refers to the protein first isolated from the Victoria multi-tube glowing jellyfish.This protein was first discovered by xiu shimura et al. in 1962 in the Victoria multi-tube glowing jellyfish.The luminescence process also requires the help of the luminescent protein medusin, which interacts with calcium ions. Green fluorescent protein (Green fluorescent protein, GFP), is a composed of about 238 amino acid protein, can make its excitation from blue to ultraviolet ray, a Green fluorescence.While many other Marine organisms have similar GFP proteins, traditionally GFP refers to the protein first isolated from the Victoria multi-tube glowing jellyfish.This protein was first discovered by xiu shimura et al. in 1962 in the Victoria multi-tube glowing jellyfish.The luminescence process also requires the help of the luminescent protein medusin, which interacts with calcium ions. The wild-type green fluorescent protein found in the Victoria multi-tube luminescent jellyfish has the largest and sublargest excitation wavelengths at 395nm and 475nm respectively, and its emission wavelength peaks at 509nm, and it is in the position of green light bluish in the visible spectrum.The fluorescence quantum yield (QY) of green fluorescent protein was 0.79.However, the GFP obtained from sea pansy had a high excitation peak at 498nm. Structure of Green Fluorescent Protein

2. Wild-type green fluorescent protein started with 238 amino acid peptides, approximately 25KDa.Then, according to certain rules, 11 -folded outer perimeter cylindrical fence;In a cylinder, alpha - helix holds the chromophore almost to the center.The chromatogram is enclosed in the center, which can avoid dipolar water molecules, paramagnetic oxygen molecules or cis-trans isomerization and chromophore, resulting in fluorescence quenching. Fluorescence is the most distinctive feature of fluorescent proteins, and the chromophore plays a major role.The amino acids (serine, tyrosine, glycine) at positions 65, 66, and 67 on -helix are cycle-bound and dehydrogenated to form chromophore.Interestingly, chromophore formation is catalyzed by residues on the perimeter fence, and the substrate only needs oxygen.This suggests the potential for green fluorescent proteins to be widely used in different species: they can be independently expressed as functional proteins in different species without the need for additional factors.But the exact process is still being discussed. The conjugate PI bond on the chromophore absorbs excited light energy, which is released in a longer wavelength after a very short time to form fluorescence. Application of Green Fluorescent Protein Since fluorescent proteins can be inherited stably in the offspring and can be expressed specifically according to the promoter, they have gradually replaced the traditional chemical dyes in quantitative or other experiments.More often, fluorescent proteins have been engineered into different new tools, offering new ideas for solving problems and potentially more valuable ones. The availability of GFP and its derivatives has radically redefined fluorescence microscopy, as well as the way it is used in cell biology and other biological disciplines.One of the most exciting is superresolution microscope imaging.