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GFP-like proteins

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GFP-like proteins constitute a fast growing family as several naturally occurring GFP-like proteins have been discovered and enhanced mutants of Aequorea GFP have been created.
Evidence 1Source 1DOIPubMedprovenance

Supporting Sources

Linked Claims

Claim 1application scopesupports2008Source 1DOIPubMed

The review summarizes GFP-like protein utilization as markers and biosensors in cell and molecular biology.

Quoted textsource-backed
This review is an attempt to characterize the main color groups of GFP-like proteins, describe their structure and mechanisms of chromophore formation, systemize data on their conformational stability and summarize the main trends of their utilization as markers and biosensors in cell and molecular biology.
Claim 2color palettesupports2008Source 1DOIPubMed

GFP-like proteins span multiple emission classes including green, blue, orange-red, far-red, cyan, and yellow, and can also show dual-color fluorescence or be non-fluorescent.

Quoted textsource-backed
GFP-like proteins are very diverse, as they can be not only green, but also blue, orange-red, far-red, cyan, and yellow. They also can have dual-color fluorescence (e.g., green and red) or be non-fluorescent.
Claim 3family diversitysupports2008Source 1DOIPubMed

GFP-like proteins form a rapidly growing family that includes naturally occurring proteins and engineered mutants of Aequorea GFP.

Quoted textsource-backed
GFP-like proteins constitute a fast growing family as several naturally occurring GFP-like proteins have been discovered and enhanced mutants of Aequorea GFP have been created.
Claim 4photochemical classsupports2008Source 1DOIPubMed

Within GFP-like proteins, some members are kindling, some are photoactivatable, and some are photoswitchable.

Quoted textsource-backed
Some of them possess kindling property, some are photoactivatable, and some are photoswitchable.
Claim 5property variationsupports2008Source 1DOIPubMed

Engineered GFP mutants differ from wild-type GFP in conformational stability, quantum yield, spectroscopic properties, and photochemical properties.

Quoted textsource-backed
These mutants differ from wild-type GFP by conformational stability, quantum yield, spectroscopic properties (positions of absorption and fluorescence spectra) and by photochemical properties.