An ultrafast polarisation spectroscopy study of internal conversion and orientational relaxation of the chromophore of the green fluorescent protein

Litvinenko, K. L.; Webber, Naomi M.; Meech, Stephen R.

doi:10.1016/s0009-2614(01)00938-1

Cited by 51 publications

(77 citation statements)

References 31 publications

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“…1), which causes nonradiative decay of the excited state. [38][39][40][41] In these model compounds, the excited state can adopt a twisted conformation in which fluorescence quenching can occur through nonadiabatic crossing. We hypothesize that the oxygen of the donor carbonyl group restrains the imidazolidinone ring of the chromophore in the rigid state that is necessary for its unusual photophysical properties, deterring the attainment of the deleterious twisted conformation.…”

Section: -27mentioning

confidence: 99%

A conserved interaction with the chromophore of fluorescent proteins

2011

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The chromophore of fluorescent proteins, including the green fluorescent protein (GFP), contains a highly conjugated imidazolidinone ring. In many fluorescent proteins, the carbonyl group of the imidazolidinone ring engages in a hydrogen bond with the side chain of an arginine residue. Prior studies have indicated that such an electrophilic carbonyl group in a protein often accepts electron density from a main-chain oxygen. A survey of high-resolution structures of fluorescent proteins indicates that electron lone pairs of a main-chain oxygen-Thr62 in GFP-donate electron density into an antibonding orbital of the imidazolidinone carbonyl group. This nfip* electron delocalization prevents structural distortion during chromophore excitation that could otherwise lead to fluorescence quenching. In addition, this interaction is present in on-pathway intermediates leading to the chromophore, and thus could direct its biogenesis. Accordingly, this nfip* interaction merits inclusion in computational and photophysical analyses of the chromophore, and in speculations about the molecular evolution of fluorescent proteins.

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Section: -27mentioning

confidence: 99%

A conserved interaction with the chromophore of fluorescent proteins

2011

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“…2 lacks the barrier probably because the amino acid surrounding the chromophore was not taken into account. The hula-twist mechanism also explains the weak dependence of the GFP's chromophore fluorescence decay time on the viscosity of the solvent [15,16]. The fact, that neutral chromophore of GFP has a twisted conformation in the excited state, has been confirmed by femtosecond polarization-sensitive mid-infrared spectroscopy [17].…”

Section: Resultsmentioning

confidence: 79%

Photophysics of the blue fluorescent protein

Mauring

Krasnenko

Miller

2007

Journal of Luminescence

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“…relative to avgFP (quantum yield about 0.8), hBdi is very weakly fluorescent (fluorescent quantum yield 10 −4 ) in aqueous solution at room temperature [44]. Ultrafast spectroscopy of hBdi reveals that highly efficient internal conversion occurs in a wide range of solvents leading to deactivation of the excited state on a subpicosecond time scale, which is too short for fluorescence to be a competitive process [45][46][47]. in contrast, avgFP displays excited-state lifetimes of about 3 ns.…”

Section: Chromophore Environment and Fluorescence Emissionmentioning

confidence: 99%

Fluorescent Proteins for Neuronal Imaging

Zhao

Campbell

2015

Biological and Medical Physics, Biomedical Engineering

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over the past two decades, the growing selection of engineered fluorescent proteins have helped drive a revolution in the ability of researchers to image protein localization and biochemical dynamics in live cells in real time. although the fluorescent proteins were long preceded by other fluorophores compatible with live cell imaging, the fact that fluorescent proteins are fully genetically encoded has enabled them to be applied in applications that would not otherwise be possible. in particular, fluorescent proteins have enabled the creation of transgenic animals in which specific neuronal cell types are uniquely and fluorescently labeled. Furthermore, through the use of highly engineered fluorescent proteins that change their fluorescence in response to a change in calcium ion concentration or membrane potential, fluorescent proteins have enabled high resolution minimally invasive imaging of neuronal activity in model organisms. in this chapter we will provide an overview of fluorescent protein technology and detail the technological developments that have made such experiments possible. Particular emphasis will be placed on the development of strategies for engineering ca 2+ and voltage indicators, and the latest breakthroughs in these directions will be highlighted.

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An ultrafast polarisation spectroscopy study of internal conversion and orientational relaxation of the chromophore of the green fluorescent protein

Cited by 51 publications

References 31 publications

A conserved interaction with the chromophore of fluorescent proteins

A conserved interaction with the chromophore of fluorescent proteins

Photophysics of the blue fluorescent protein

Fluorescent Proteins for Neuronal Imaging

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