2008年8月25日 · Despite their pronounced spectral variability, coloration of GFP-like proteins is attained through a fairly conserved mechanism. Wild-type proteins of the GFP family have an 11-stranded β barrel structure (Figure 1 A), with the conservative tyrosine and glycine residues in a chromogenic X-Tyr-Gly amino acid sequence.After polypeptide folding, the protein undergoes maturation via consecutive ...

The GFP family and its mutants From the perspective of its usefulness in the biosciences, some aspects of GFP function stand out. Among these are: (i) the brightness of the molecule, defined as the extinction coefficient at the maximum of the excitation spectrum (see Fig. 1) multiplied by the quantum yield, i.e.

Members of the family of the Green Fluorescent Protein (GFP) are the only known type of natural pigments that are essentially encoded by a single gene, since both the substrate for pigment biosynthesis and the necessary catalytic moieties are provided within a single polypeptide chain. In sharp contrast to the state of knowledge just three ...

2008年7月3日 · Members of the green fluorescent protein (GFP) family share sequence similarity and the 11-stranded β-barrel fold. Fluorescence or bright coloration, observed in many members of this family, is enabled by the intrinsic properties of the polypeptide chain itself, without the requirement for cofactors. Amino acid sequence of fluorescent proteins can be altered by genetic engineering to produce ...

2008年8月25日 · Proteins homologous to green fluorescent protein (GFP) span most of the visible spectrum, offering indispensable tools for live cell imaging. Structural transformations, such as posttranslational autocatalytic and photo-induced modifications, chromophore isomerization, and rearrangements in its envi …

2008年8月25日 · The GFP family consists of homologous proteins from marine organisms that contain chromophores derived from their internal amino acids. Most GFP-like proteins display bright fluorescence, with their optical properties encoded genetically and the chromophore center assembled posttranslationally by autocatalytic reactions inside the protein shell.

2004年5月1日 · Introduction. Green fluorescent protein (GFP) along with its mutants and homologs are widely known today because of their extensive use as in vivo fluorescent markers facilitating biomedical studies (Tsien 1998; Lippincott-Schwartz and Patterson 2003).Investigation of this protein family began more than 40 years ago when GFP from hydromedusa Aequorea victoria (synonym A. aequorea) was ...

the GFP family (Barondeau et al., 2007). Together, these data also imply that Tyr66 controls proper oxidative chemistry in p-HBI chromophore biosynthesis. The founding member of the family, avGFP (green fluorescent protein from Aequorea victoria), absorbs light at 395 nm, with a smaller peak at 475 nm, and emits green light at 508 nm. The

2002年4月2日 · The family of proteins homologous to the green fluorescent protein (GFP) from Aequorea victoria exhibits striking diversity of features, including several different types of autocatalytically synthesized chromophores. Here we report 11 new members of the family, among which there are 3 red-emitters possessing unusual features, and discuss the similarity relationships within the family in ...

2011年1月1日 · The green fluorescent protein (GFP) and the related fluorescent proteins (FPs) of the GFP family have revolutionized life sciences research by enabling a vast array of novel approaches to study biomolecular processes, especially in living cells and organisms.