Spectroscopic Proximity Sensor
Spectroscopic Proximity Sensor - Related Videos
09:14
Glovebox and Impurity Sensors
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2023
Source: Tamara M. Powers, Department of Chemistry, Texas A&M University The glovebox provides a straightforward means to handle air- and moisture-sensitive solids and liquids. The glovebox is what it sounds like: a box with gloves attached to one or more sides, which allows the user to perform manipulations within the glovebox under an inert atmosphere. For manipulations under inert atmospheres, chemists can choose between Schlenk or high-vacuum techniques and a glovebox. Schlenk and...
13:06
Visualization of miniSOG Tagged DNA Repair Proteins in Combination with Electron Spectroscopic Imaging (ESI)
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Cited by 12 •
2015
Electron spectroscopic imaging can image and distinguish nucleic acid from protein at nanometer resolution. It can be combined with the miniSOG system, which is able to specifically label tagged proteins in transmission electron microscopy samples. We illustrate the use of these technologies using double-strand break repair foci as an example.
10:41
Method to Measure Tone of Axial and Proximal Muscle
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Cited by 5 •
2011
We have developed a device (Twister) to study the regulation of tonic muscle activity during active postural maintenance. Twister measures torsional resistance and muscular responses in standing subjects during twisting of the body axis. The device can be flexibly configured to study various aspects of tonic control across the neck, trunk, and/or hips.
06:23
Modeling Hypoxia/Reoxygenation Injury in Proximal Tubular Epithelial Cells
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2025
Here, we describe an in vitro protocol to model hypoxia/reoxygenation damage in the highly metabolic proximal tubular epithelial cells. This model is designed to induce metabolic stress-induced damage, which can be measured through the expression of proximal tubule damage markers and assessment of mitochondrial respiratory function.
09:30
Bacterial Detection & Identification Using Electrochemical Sensors
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Cited by 6 •
2013
We describe an electrochemical sensor assay method for rapid bacterial detection and identification. The assay involves a sensor array functionalized with DNA oligonucleotide capture probes for ribosomal RNA (rRNA) species-specific sequences. Sandwich hybridization of target rRNA with the capture probe and a horseradish peroxidase-linked DNA oligonucleotide detector probe produces a measurable amperometric current.
FAQs
The key variable is the donor–acceptor separation. When labeled molecular regions move closer, energy transfer from the excited fluorescent donor to the acceptor changes the measured fluorescence. Because the signal responds at nanometer-scale distances, shifts in optical output can indicate molecular rearrangement rather than merely showing that both labels are present.
FRET readouts can be tracked through fluorescence intensity or an emission ratio, giving two related ways to represent proximity changes. A rising or falling signal is interpreted in relation to the labeled pair’s separation, so the measurement can follow distance changes during binding or conformational transitions instead of providing only an endpoint observation.
Label placement determines which molecular distance the sensor reports. Labels may be attached to two molecules or to selected molecular regions, allowing the optical response to represent an interaction between partners or a structural change within one system. This makes the same sensing principle adaptable to protein–protein interactions, ligand binding, and enzyme-associated conformational changes.
A basic experiment starts by selecting labeled molecules or regions whose proximity is biologically meaningful. The donor is excited, and fluorescence intensity or an emission ratio is monitored as the system changes. Researchers then relate the optical change to molecular separation, using the result to examine interactions, binding, or conformational dynamics.
In enzyme-focused biochemistry, the sensor can report conformational changes associated with enzyme activity or molecular association, while ligand-binding studies can use proximity changes as an optical readout of recognition. The value is mechanistic: measurements connect a biochemical event to nanoscale molecular organization, helping researchers examine how structural changes accompany function.
Within cells, these probes can follow signaling-related proximity changes in real time while molecular organization changes. This makes them relevant to intracellular signaling research, where dynamic optical measurements can be related to biochemical events. The resulting data provide quantitative insight into molecular organization and dynamics, supporting biosensor development and mechanistic studies.