Over the last decades, fluorescent proteins (FPs) have been extensively employed for imaging and tracing in cell-biology and medicine. However, their application for lighting devices like light-emitting diodes (LEDs) and lasers has recently started. The interest of FPs lies on their good photoluminescence features (high emission efficiency with a narrow spectrum and a high photon flux saturation), good photostability, low-cost production via bacteria, and eco-friendly recycling. The low stability at high temperatures as well as the need of an aqueous environment have, however, strongly limited their use in optoelectronics. This has recently been circumvented with new coating systems that are paving the way for the entrance of FPs into the LED field. In this minireview, we summarize the first steps done by a few groups towards the development of bio-inspired hybrid white LEDs (Bio-HWLEDs) with a focus on using FPs as color down-converters, highlighting the state-of-the-art and challenges associated to this emerging field.
Chromophore Isomer Stabilization Is Critical to theEfficient Fluorescence of Cyan Fluorescent Proteins
Chromophore Isomer Stabilization Is Critical to theEfficient Fluorescence of Cyan Fluorescent Proteins
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b01088/20171127/images/medium/bi-2017-01088f_0006.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b01088
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11-28-2017 03:58 AM
[NMR paper] Rational Engineering of Photoconvertible Fluorescent Proteins for Dual-Color Fluorescence Nanoscopy Enabled by a Triplet-State Mechanism of Primed Conversion
Rational Engineering of Photoconvertible Fluorescent Proteins for Dual-Color Fluorescence Nanoscopy Enabled by a Triplet-State Mechanism of Primed Conversion
Green-to-red photoconvertible fluorescent proteins (pcFPs) are powerful tools for super-resolution localization microscopy and protein tagging. Recently, they have been found to undergo efficient photoconversion not only by the traditional 400-nm illumination but also by an alternative method termed primed conversion, employing dual wavelength illumination with blue and far-red/near-infrared light. Primed conversion has been...
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07-12-2017 12:48 AM
[NMR paper] A triplet state mechanism of primed conversion enables rational engineering of photoconvertible fluorescent proteins for dual color fluorescence nanoscopy
A triplet state mechanism of primed conversion enables rational engineering of photoconvertible fluorescent proteins for dual color fluorescence nanoscopy
Photoconvertible fluorescent proteins (pcFPs) are powerful tools for super-resolution localization microscopy and protein tagging. Recently, they have been found to undergo efficient photoconversion by an alternative method termed primed conversion, employing dual wavelength illumination with blue and far-red/near-infrared light. Primed conversion has been reported only for Dendra2 and its mechanism has remained elusive. Here, we...
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06-30-2017 05:34 AM
[NMR paper] A general mechanism of photoconversion of green-to-red fluorescent proteins based on blue and infrared light reduces phototoxicity in live-cell single-molecule imaging
A general mechanism of photoconversion of green-to-red fluorescent proteins based on blue and infrared light reduces phototoxicity in live-cell single-molecule imaging
Photoconversion of fluorescent proteins by blue and complementary near-infrared light, termed primed conversion (PC), is a mechanism recently discovered for Dendra2. We demonstrate that controlling the conformation of arginine at residue 66 by threonine at residue 69 of fluorescent proteins from Anthozoan families (Dendra2, mMaple, Eos, mKikGR, pcDronpa protein families) represents a general route to facilitate PC....
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06-02-2017 08:33 PM
In vivo Imaging Fluorescent Proteins Expressed from DNA Vaccine Constructs - News-Medical.net
In vivo Imaging Fluorescent Proteins Expressed from DNA Vaccine Constructs - News-Medical.net
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In vivo Imaging Fluorescent Proteins Expressed from DNA Vaccine Constructs
News-Medical.net
Nevertheless, most of the clinical trials that reported the use of these proteins have used recombinant viruses; injected cells expressing the proteins; or used recombinant protein in an artificial mouse. This article examines the technique used to ...
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12-17-2013 01:46 PM
[NMR paper] Bioconjugation of proteins with a paramagnetic NMR and fluorescent tag.
Bioconjugation of proteins with a paramagnetic NMR and fluorescent tag.
Related Articles Bioconjugation of proteins with a paramagnetic NMR and fluorescent tag.
Chemistry. 2013 Dec 9;19(50):17141-9
Authors: Huang F, Pei YY, Zuo HH, Chen JL, Yang Y, Su XC
Abstract
Site-specific labeling of proteins with lanthanide ions offers great opportunities for investigating the structure, function, and dynamics of proteins by virtue of the unique properties of lanthanides. Lanthanide-tagged proteins can be studied by NMR, X-ray, fluorescence, and EPR...
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12-07-2013 01:00 PM
A natural and readily available crowding agent: NMR studies of proteins in hen egg white.
A natural and readily available crowding agent: NMR studies of proteins in hen egg white.
A natural and readily available crowding agent: NMR studies of proteins in hen egg white.
Proteins. 2010 Dec 13;
Authors: Martorell G, Adrover M, Kelly G, Temussi PA, Pastore A
In vitro studies of biological macromolecules are usually performed in dilute, buffered solutions containing one or just a few different biological macromolecules. Under these conditions, the interactions among molecules are diffusion limited. On the contrary, in living systems,...
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02-22-2011 10:40 PM
[NMR paper] 1H-NMR analysis of turkey egg-white lysozyme and comparison with hen egg-white lysozy
1H-NMR analysis of turkey egg-white lysozyme and comparison with hen egg-white lysozyme.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles 1H-NMR analysis of turkey egg-white lysozyme and comparison with hen egg-white lysozyme.
Eur J Biochem. 1993 Jul 15;215(2):255-66
Authors: Bartik K, Dobson CM, Redfield C
The complete main chain and approximately 75% of the side chain 1H-NMR assignments of the 129-residue protein, turkey...