Laser-Excited One-Atom Source of Electrons

1997 ◽  
Vol 06 (04) ◽  
pp. 411-420
Author(s):  
V. S. Letokhov ◽  
S. K. Sekatskii
Keyword(s):  
Calcium Fluoride ◽  
Lithium Fluoride ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Fluorescence Yield ◽  
Color Centers ◽  
Light Sources ◽  
Microscopy Technique ◽  
Atom Source ◽  
High Fluorescence

A finite number of color centers in the region of sharp crystal needle's tip has been recently observed by laser resonance photoelectron projection microscopy technique. Hereby we present a new result in the field: only one single color center was observed on the tip region of lithium fluoride and calcium fluoride needles. Due to the high fluorescence yield of these color centers such needles can be treated as one-atom light sources, and perspectives of their application in Scanning One-Atom Fluorescence Resonance Energy Transfer Microscopy are briefly discussed.

scholarly journals “Where does the fluorescing moiety reside in a carbon dot?” – Investigations based on fluorescence anisotropy decay and resonance energy transfer dynamics

2018 ◽  
Vol 20 (4) ◽  
pp. 2251-2259 ◽  
Author(s):  
Ananya Das ◽  
Debjit Roy ◽  
Chayan K. De ◽  
Prasun K. Mandal
Keyword(s):  
Energy Transfer ◽  
Fluorescence Anisotropy ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Fluorescence Anisotropy Decay ◽  
Carbon Dot ◽  
Anisotropy Decay ◽  
High Fluorescence ◽  
Very High

It has been shown recently that aggregated dyes are responsible for very high fluorescence in a carbon dot (CD). Location of the fluorescing unit in a carbon dot could be shown.

scholarly journals Designing a Compact, Low-Cost FRET Microscopy Platform for the Undergraduate Classroom

2020 ◽  
Vol 1 (2) ◽  
Author(s):  
John W. Rupel ◽  
Sophia M. Sdao ◽  
Kadina E. Johnston ◽  
Ethan T. Nethery ◽  
Kaitlyn A. Gabardi ◽  
...  
Keyword(s):  
Undergraduate Students ◽  
Fluorescent Protein ◽  
Dynamic Range ◽  
Low Cost ◽  
Yellow Fluorescent Protein ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Light Sources ◽  
Effective Manner ◽  
Primary Mouse

ABSTRACT Advances in fluorescent biosensors allow researchers to spatiotemporally monitor a diversity of biochemical reactions and secondary messengers. However, commercial microscopes for the specific application of Förster Resonance Energy Transfer (FRET) are prohibitively expensive to implement in the undergraduate classroom, owing primarily to the dynamic range required and need for ratiometric emission imaging. The purpose of this article is to provide a workflow to design a low-cost, FRET-enabled microscope and to equip the reader with sufficient knowledge to compare commercial light sources, optics, and cameras to modify the device for a specific application. We used this approach to construct a microscope that was assembled by undergraduate students with no prior microscopy experience that is suitable for most single-cell cyan and yellow fluorescent protein FRET applications. The utility of this design was demonstrated by measuring small metabolic oscillations by using a lactate FRET sensor expressed in primary mouse pancreatic islets, highlighting the biologically suitable signal-to-noise ratio and dynamic range of our compact microscope. The instructions in this article provide an effective teaching tool for undergraduate educators and students interested in implementing FRET in a cost-effective manner.

scholarly journals Production of a fluorescence resonance energy transfer (FRET) biosensor membrane for microRNA detection

2017 ◽  
Vol 5 (34) ◽  
pp. 7133-7139 ◽  
Author(s):  
Yike Fu ◽  
Tong Chen ◽  
Gang Wang ◽  
Tongxu Gu ◽  
Congkun Xie ◽  
...  
Keyword(s):  
Gold Nanoparticles ◽  
Energy Transfer ◽  
Rare Earth ◽  
Calcium Fluoride ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Quantitative Methodology ◽  
Microrna Detection ◽  
Silica Nanofibers ◽  
Rare Earth Doped

A FRET biosensor, based on rare earth-doped calcium fluoride particles incorporated into silica nanofibers (CaF2:Yb,Ho@SiO2) and gold nanoparticles (AuNPs), offers a simple and quantitative methodology for miRNA-195 detection.

First characterization of the development of bleached kraft softwood pulp fiber interfaces during drying and rewetting using FRET microscopy

Holzforschung ◽  
2008 ◽  
Vol 62 (4) ◽  
Author(s):  
Cameron I. Thomson ◽  
Robert M. Lowe ◽  
Arthur J. Ragauskas
Keyword(s):  
Kraft Pulp ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Pulp Fiber ◽  
Cellulosic Fibers ◽  
Bleached Kraft Pulp ◽  
Microscopy Technique ◽  
Wet Pressing ◽  
Fiber Components ◽  
Solids Content

Abstract Cellulosic fiber interfaces are critical to the material properties of paper. Likewise, the presence of water in a paper sheet is an important property, because paper is a wet-laid structure and the cellulosic fibers that compose it are hygroscopic. This work uses a fluorescence microscopy technique established by the authors to study the development of individual bleached kraft pulp fiber crossings in situ during drying and through a cycle of rewetting and wet pressing. The results indicate that coalescence of the fiber-fiber interface occurs during drying and that the fluorescence resonance energy transfer (FRET) response, which is proportional to the distance between fiber components, increases logarithmically with time. The FRET signal of once-dried fiber crossings increases dramatically after rewetting and wet pressing for a second time. This indicates that fiber bonds are still compliant after a single drying cycle and that the interactions between fiber components are likely reversible at the solids content present in bleached kraft pulp fiber crossings dried at 25°C and 50% relative humidity.

Structural dynamics of P-type ATPase ion pumps

2019 ◽  
Vol 47 (5) ◽  
pp. 1247-1257 ◽  
Author(s):  
Mateusz Dyla ◽  
Sara Basse Hansen ◽  
Poul Nissen ◽  
Magnus Kjaergaard
Keyword(s):  
Structural Dynamics ◽  
Single Molecule ◽  
New Technologies ◽  
Atp Hydrolysis ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Time Resolved ◽  
Dynamics Simulations ◽  
Types Of Information ◽  
P Type

Abstract P-type ATPases transport ions across biological membranes against concentration gradients and are essential for all cells. They use the energy from ATP hydrolysis to propel large intramolecular movements, which drive vectorial transport of ions. Tight coordination of the motions of the pump is required to couple the two spatially distant processes of ion binding and ATP hydrolysis. Here, we review our current understanding of the structural dynamics of P-type ATPases, focusing primarily on Ca2+ pumps. We integrate different types of information that report on structural dynamics, primarily time-resolved fluorescence experiments including single-molecule Förster resonance energy transfer and molecular dynamics simulations, and interpret them in the framework provided by the numerous crystal structures of sarco/endoplasmic reticulum Ca2+-ATPase. We discuss the challenges in characterizing the dynamics of membrane pumps, and the likely impact of new technologies on the field.

Quantum Dot Bioconjugates as Energy Donors in Fluorescence Resonance Energy Transfer Assays

2003 ◽  
Vol 773 ◽  
Author(s):  
Aaron R. Clapp ◽  
Igor L. Medintz ◽  
J. Matthew Mauro ◽  
Hedi Mattoussi
Keyword(s):  
Energy Transfer ◽  
Quantum Dot ◽  
Organic Dyes ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Genetically Engineered ◽  
Molar Ratio ◽  
Binding Assays ◽  
Specific Sequence ◽  
Donor Acceptor

AbstractLuminescent CdSe-ZnS core-shell quantum dot (QD) bioconjugates were used as energy donors in fluorescent resonance energy transfer (FRET) binding assays. The QDs were coated with saturating amounts of genetically engineered maltose binding protein (MBP) using a noncovalent immobilization process, and Cy3 organic dyes covalently attached at a specific sequence to MBP were used as energy acceptor molecules. Energy transfer efficiency was measured as a function of the MBP-Cy3/QD molar ratio for two different donor fluorescence emissions (different QD core sizes). Apparent donor-acceptor distances were determined from these FRET studies, and the measured distances are consistent with QD-protein conjugate dimensions previously determined from structural studies.

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