Single Protein Tracking
Single Protein Tracking - Related Videos
08:39
Tracking Single Proteins in Lipid Bilayers Using Fluorescence Microscopy
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2025
This article provides a detailed description of how to create samples for single-protein tracking in solid-supported lipid bilayers. It also explains a straightforward fluorescence microscope with single-molecule sensitivity and a fast frame rate. Finally, we outline the procedure for extracting single-protein trajectories.
16:21
Visualizing Protein-DNA Interactions in Live Bacterial Cells Using Photoactivated Single-molecule Tracking
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Cited by 38 •
2014
Photoactivated localization microscopy (PALM) combined with single-molecule tracking allows direct observation and quantification of protein-DNA interactions in live Escherichia coli cells.
07:19
Cell Tracking Using Photoconvertible Proteins During Zebrafish Development
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Cited by 17 •
2012
Here, we present a method for the photoactivated switch of photoconvertible fluorescent proteins (PCFPs) in the living zebrafish embryo and further tracking of photoconverted protein at specific time points during development. This methodology allows monitoring of cell biological events underlying different developmental processes in a live vertebrate organism.
02:53
Tracking Bacterial Growth at Single-Cell Resolution in a Microfluidic System
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2025
Source: Cabeen, M. T., et al. Single-cell Microfluidic Analysis of Bacillus subtilis. J. Vis. Exp. (2018)The video demonstrates the use of a microfluidic device to observe bacterial growth at the single-cell level. It showcases how non-motile bacterial cells, confined within micro-scale trenches, are continuously nourished and imaged under a fluorescence microscope. The setup enables real-time visualization of cell division and lineage tracking across multiple generations.
04:25
Simultaneous Eye Tracking and Single-Neuron Recording to Identify Target-Selective Neurons
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2025
The video demonstrates an assay to identify target-selective neurons via simultaneous eye-tracking and single-neuron recordings. A human participant is tasked with identifying a target object among an array of objects in a display, and the eye movement is tracked. Simultaneously, single neurons' firing rate is recorded via electrodes implanted in the brain. The data from both recordings are correlated to assess the presence of target-selective neurons.
FAQs
A trajectory converts the recorded position of one protein across successive frames into a time-resolved description of its motion. Researchers can examine whether the molecule diffuses, becomes confined, binds a partner, or undergoes transport. These distinct movement patterns connect observable dynamics with biochemical interactions and help clarify how molecular behavior changes during a process.
Ensemble measurements combine signals from many protein molecules, which can conceal differences in individual behavior. Following molecules separately preserves those differences, allowing researchers to identify distinct movement patterns within the same experiment. This molecule-level view is especially useful when proteins alternate between diffusion, confinement, binding, or transport rather than behaving uniformly.
A fluorescent marker makes the selected protein detectable, while time-resolved microscopy records its position repeatedly over time. Together, these components provide the sequential observations needed to construct a molecular trajectory. The resulting record supports quantitative analysis of movement and helps relate a protein’s behavior to its biochemical surroundings.
Single Protein Tracking can compare protein motion under different conditions, revealing changes in diffusion, confinement, binding, or transport. Such comparisons help determine whether a protein interacts with a membrane, nucleic acid, or another biomolecule, and whether those interactions alter its movement. The approach therefore links environmental changes to measurable molecular dynamics.
Researchers first label the target protein with a fluorescent marker and then use time-resolved microscopy to record its position in successive frames. They convert these positional observations into trajectories and quantify movement features such as diffusion, confinement, binding, and transport. The measurements can then be compared across conditions or related to biochemical function.
The method supports investigations of how individual proteins interact with membranes, nucleic acids, and other biomolecules. In biochemistry, those observations can clarify reaction mechanisms and molecular transport while connecting motion to function. The same information also contributes to studies of cellular organization and to the investigation of proteins relevant to therapeutic targets.