Controlling fluorescent proteins by manipulating the local density of photonic states

2009 ◽  
Author(s):  
Christian Bluma ◽  
Yanina Cesa ◽  
Johanna M. van den Broek ◽  
Allard P. Mosk ◽  
Willem L. Vos ◽  
...  
Keyword(s):  
Fluorescent Proteins ◽  
Local Density ◽  
Photonic States

Controlling fluorescent proteins by manipulating the local density of photonic states

2009 ◽  
Author(s):  
Christian Blum ◽  
Yanina Cesa ◽  
Johanna M. van den Broek ◽  
Allard P. Mosk ◽  
Willem L. Vos ◽  
...  
Keyword(s):  
Fluorescent Proteins ◽  
Local Density ◽  
Photonic States

Analysis of the Limits of the Local Density of Photonic States near Nanostructures

ACS Photonics ◽  
2018 ◽  
Vol 5 (6) ◽  
pp. 2437-2445 ◽  
Author(s):  
Stephen Sanders ◽  
Alejandro Manjavacas
Keyword(s):  
Local Density ◽  
Photonic States

scholarly journals Scanning Single Quantum Emitter Fluorescence Lifetime Imaging: Quantitative Analysis of the Local Density of Photonic States

Nano Letters ◽  
2014 ◽  
Vol 14 (5) ◽  
pp. 2623-2627 ◽  
Author(s):  
Andreas W. Schell ◽  
Philip Engel ◽  
Julia F. M. Werra ◽  
Christian Wolff ◽  
Kurt Busch ◽  
...  
Keyword(s):  
Quantitative Analysis ◽  
Fluorescence Lifetime ◽  
Local Density ◽  
Fluorescence Lifetime Imaging ◽  
Single Quantum ◽  
Lifetime Imaging ◽  
Quantum Emitter ◽  
Photonic States

Manipulation of the local density of photonic states to elucidate fluorescent protein emission rates

2009 ◽  
Vol 11 (14) ◽  
pp. 2525 ◽  
Author(s):  
Yanina Cesa ◽  
Christian Blum ◽  
Johanna M. van den Broek ◽  
Allard P. Mosk ◽  
Willem L. Vos ◽  
...  
Keyword(s):  
Fluorescent Protein ◽  
Local Density ◽  
Emission Rates ◽  
Photonic States

Relationship between scanning near-field optical images and local density of photonic states

2001 ◽  
Vol 345 (5-6) ◽  
pp. 512-516 ◽  
Author(s):  
Gérard Colas des Francs ◽  
Christian Girard ◽  
Jean-Claude Weeber ◽  
Alain Dereux
Keyword(s):  
Local Density ◽  
Near Field ◽  
Optical Images ◽  
Photonic States

MODE TUNING IN PHOTONIC CRYSTAL CAVITIES USING GEOMETRY OF FIRST NEIGHBORING LAYER

2012 ◽  
Vol 21 (04) ◽  
pp. 1250048 ◽  
Author(s):  
AZARDOKHT MAZAHERI ◽  
HAMID REZA FALLAH ◽  
JAVAD ZARBAKHSH
Keyword(s):  
Photonic Crystal ◽  
Strong Influence ◽  
Local Density ◽  
Optical Source ◽  
Photonic Crystal Cavities ◽  
Frequency Distributions ◽  
Neighboring Layer ◽  
Cavity Modes ◽  
Spectral Distributions ◽  
Photonic States

The relation between position of optical source and excitation of photonic crystal cavity modes are investigated. For multimode cavities, the source position considerably affects the modes' excitation. The frequency distributions of local density of photonic states in a multimode cavity differ for source positions at structural symmetric locations and nonsymmetrical ones. It was also found that the geometry of cavity's neighboring layers has strong influence on the spatial and spectral distributions of modes. The results also show that the shifts of various cavity modes in frequency domain have different sensitivity with respect to geometrical tolerance. This can be used in various applications which need mode tuning.

Ab initio band theory approach to electron energy loss near edge structures

1988 ◽  
Vol 46 ◽  
pp. 506-507
Author(s):  
Xudong Weng ◽  
O.F. Sankey ◽  
Peter Rez
Keyword(s):  
Ab Initio ◽  
Local Density ◽  
Interpolation Method ◽  
Atomic Orbital ◽  
Plane Waves ◽  
Large Set ◽  
Theory Approach ◽  
Band Theory ◽  
Atomic Orbitals ◽  
Pseudopotential Calculations

Single electron band structure techniques have been applied successfully to the interpretation of the near edge structures of metals and other materials. Among various band theories, the linear combination of atomic orbital (LCAO) method is especially simple and interpretable. The commonly used empirical LCAO method is mainly an interpolation method, where the energies and wave functions of atomic orbitals are adjusted in order to fit experimental or more accurately determined electron states. To achieve better accuracy, the size of calculation has to be expanded, for example, to include excited states and more-distant-neighboring atoms. This tends to sacrifice the simplicity and interpretability of the method.In this paper. we adopt an ab initio scheme which incorporates the conceptual advantage of the LCAO method with the accuracy of ab initio pseudopotential calculations. The so called pscudo-atomic-orbitals (PAO's), computed from a free atom within the local-density approximation and the pseudopotential approximation, are used as the basis of expansion, replacing the usually very large set of plane waves in the conventional pseudopotential method. These PAO's however, do not consist of a rigorously complete set of orthonormal states.

Flux-pinning-related defect structures in melt-processed YBa2Cu3O7-x

1993 ◽  
Vol 51 ◽  
pp. 936-937
Author(s):  
Z. L. Wang ◽  
R. Kontra ◽  
A. Goyal ◽  
D. M. Kroeger ◽  
L.F. Allard
Keyword(s):  
Volume Fraction ◽  
Local Density ◽  
Stacking Faults ◽  
Image Resolution ◽  
Defect Structures ◽  
Atomic Structures ◽  
Transmission Electron ◽  
Point Image ◽  
Related Defect ◽  
Point To Point

Previous studies of Y2BaCuO5/YBa2Cu3O7-δ(Y211/Y123) interfaces in melt-processed and quench-melt-growth processed YBa2Cu3O7-δ using high resolution transmission electron microscopy (HRTEM) and energy dispersive X-ray spectroscopy (EDS) have revealed a high local density of stacking faults in Y123, near the Y211/Y123 interfaces. Calculations made using simple energy considerations suggested that these stacking faults may act as effective flux-pinners and may explain the observations of increased Jc with increasing volume fraction of Y211. The present paper is intended to determine the atomic structures of the observed defects. HRTEM imaging was performed using a Philips CM30 (300 kV) TEM with a point-to-point image resolution of 2.3 Å. Nano-probe EDS analysis was performed using a Philips EM400 TEM/STEM (100 kV) equipped with a field emission gun (FEG), which generated an electron probe of less than 20 Å in diameter.Stacking faults produced by excess single Cu-O layers: Figure 1 shows a HRTEM image of a Y123 film viewed along [100] (or [010]).

Fluorescent proteins for in vivo imaging, where's the biliverdin?

2020 ◽  
Vol 48 (6) ◽  
pp. 2657-2667
Author(s):  
Felipe Montecinos-Franjola ◽  
John Y. Lin ◽  
Erik A. Rodriguez
Keyword(s):  
Hydrogen Peroxide ◽  
In Vivo Imaging ◽  
Near Infrared ◽  
Fluorescent Protein ◽  
Fluorescent Proteins ◽  
Fluorescent Imaging ◽  
Infrared Light ◽  
Red Fluorescent Protein ◽  
Color Palette

Noninvasive fluorescent imaging requires far-red and near-infrared fluorescent proteins for deeper imaging. Near-infrared light penetrates biological tissue with blood vessels due to low absorbance, scattering, and reflection of light and has a greater signal-to-noise due to less autofluorescence. Far-red and near-infrared fluorescent proteins absorb light >600 nm to expand the color palette for imaging multiple biosensors and noninvasive in vivo imaging. The ideal fluorescent proteins are bright, photobleach minimally, express well in the desired cells, do not oligomerize, and generate or incorporate exogenous fluorophores efficiently. Coral-derived red fluorescent proteins require oxygen for fluorophore formation and release two hydrogen peroxide molecules. New fluorescent proteins based on phytochrome and phycobiliproteins use biliverdin IXα as fluorophores, do not require oxygen for maturation to image anaerobic organisms and tumor core, and do not generate hydrogen peroxide. The small Ultra-Red Fluorescent Protein (smURFP) was evolved from a cyanobacterial phycobiliprotein to covalently attach biliverdin as an exogenous fluorophore. The small Ultra-Red Fluorescent Protein is biophysically as bright as the enhanced green fluorescent protein, is exceptionally photostable, used for biosensor development, and visible in living mice. Novel applications of smURFP include in vitro protein diagnostics with attomolar (10−18 M) sensitivity, encapsulation in viral particles, and fluorescent protein nanoparticles. However, the availability of biliverdin limits the fluorescence of biliverdin-attaching fluorescent proteins; hence, extra biliverdin is needed to enhance brightness. New methods for improved biliverdin bioavailability are necessary to develop improved bright far-red and near-infrared fluorescent proteins for noninvasive imaging in vivo.

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