infrared fluorescent protein
May 08, 2009 · Fig. 1. Infrared fluorescent proteins created by structure-based engineering of a bacteriophytochrome. (A) 14 residues surrounding the biliverdin (violet) in DrCBD (PDB ID: 1ztu) (14) were divided into 7 groups (shown in different colors) and targeted for mutagenesis.
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A molecular evolution approach enabled us to develop an advanced near-infrared fluorescent protein with excitation and emission maxima inside of the near-infrared window. We expect that this genetically encoded iRFP probe will be a valuable tool for in vivo studies in small mammals.
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Proteins for in vivo imaging have emission near or above 650 nm as signals below 650 nm are highly absorbed by hemoglobin and cause undesirable background signals. Near-infrared fluorescent proteins for in vivo imaging are derived from bacterial phytochrome photoreceptors (BphPs).
Abstract. Near-infrared fluorescent proteins are in high demand for in vivo imaging. We developed four spectrally distinct fluorescent proteins, iRFP670, iRFP682, iRFP702, and iRFP720, from bacterial phytochromes. iRFPs exhibit high brightness in mammalian …
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Near-infrared fluorescent protein (iRFP) is an engineered version of the bacteriophytochrome RpBhP2 from the bacteria Rhodopseudomonas palustris. Like other fluorescent proteins, it emits a distinct wavelength of light (peak at 713 nm) after excitation at an appropriate wavelength (peak at 690 nm).
Abstract. Infrared fluorescent proteins (IFPs) are ideal for in vivo imaging, and monomeric versions of these proteins can be advantageous as protein tags or for sensor development. In contrast to GFP, which requires only molecular oxygen for chromophore maturation, phytochrome-derived IFPs incorporate biliverdin (BV) as the chromophore.
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The quest for an infrared fluorescent protein has preoccupied several labs for a decade. Efforts to push FPs out to the infrared resulted in mCherry, mPlum, mKate, among others. The further red-shifting of these proteins is constrained by the space limitations of the beta-barrel structure of GFP-like proteins.
Development of near-infrared (NIR) fluorescent proteins (FPs) is a major focus of the FP engineering field now. Use of NIR light, in comparison to shorter-wavelength light (<640 nm), results in substantially reduced animal tissue absorbance, autofluorescence, and light-scattering.
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Modeling structure and excitation of biliverdin-binding domains in infrared fluorescent proteins. Igor V. Polyakov, Bella L. Grigorenko, Vladimir A. Mironov, Alexander V. Nemukhin. Chemical Physics Letters 2018 710, 59-63. Light-controllable Transcription System by …
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ﬂuorescent proteins engineered from 1 bacterial phytochromes Daria 1 M Shcherbakova , Mikhail Baloban1 and Vladislav V Verkhusha ,2 of near-infrared fluorescent proteins (NIR FPs) engineered from bacterial phytochrome photoreceptors (BphPs) and their chromophore photochemistry.
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Not surprisingly the best red and infrared fluorescent proteins have come from the Tsien labs. In the May 8th 2009 issue of Science a new class of IFPs was described. They are based on bacterial phytochromes, not jellyfish GFPs. Bacterial phytochromes do not normally fluorescence, instead they absorb light and then use