Tandem In Time
Tandem In Time - Related Videos
07:09
Tandem Mass Spectrometry
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2023
In tandem mass spectrometry a biomolecule of interest is isolated from a biological sample, and then fragmented into multiple subunits in order to help elucidate its composition and sequence. This is accomplished by having mass spectrometers in series. The first spectrometer ionizes a sample and filter ions of a specific mass to charge ratio. Filtered ions are then fragmented and passed to a second mass spectrometer where the fragments are analyzed. This video introduces the principles of...
01:21
Tandem Mass Spectrometry
0 Views •
2025
Tandem mass spectrometry is a technique that uses multiple mass analyzers in series to obtain a higher selectivity and reduce chemical noise during analyte detection. Instruments with multiple analyzers separated by an interaction cell enable secondary fragmentation and selected study of the fragment ions.Secondary fragmentations occur in the interaction cell and can be induced by various factors. Fragmentation induced by collision with inert gases, such as N2, Ar, He, etc., is called...
10:02
Identification of Protein Interacting Partners Using Tandem Affinity Purification
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Cited by 20 •
2012
Tandem affinity purification is a robust approach for the identification of protein binding partners. As proof of concept, this methodology was applied to the well-characterized translation initiation factor eIF4E to co-precipitate the host cell factors involved in translation initiation. This method is easily adapted to any cellular or viral protein.
11:30
Tandem Affinity Purification of Protein Complexes from Eukaryotic Cells
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Cited by 7 •
2017
We describe here a novel, robust, and efficient tandem affinity purification (TAP) method for the expression, isolation, and characterization of protein complexes from eukaryotic cells. This protocol could be utilized for the biochemical characterization of discrete complexes as well as the identification of novel interactors and post-translational modifications that regulate their function.
03:01
Detection of Fish Pathogens Using Variable Number Tandem Repeat (VNTR) Analysis
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2025
Source: Gulla, S., et al. Multi-locus Variable-number Tandem-repeat Analysis of the Fish-pathogenic Bacterium Yersinia ruckeri by Multiplex PCR and Capillary Electrophoresis. J. Vis. Exp. (2019).This video demonstrates the procedure for separating fluorescently labeled variable number tandem repeat (VNTR) amplicons, derived from a fish-pathogenic bacterium, using capillary electrophoresis to generate size-specific electropherogram profiles for bacterial identification.
FAQs
An ion trap provides the sequence needed for Tandem In Time analysis by retaining control over the selected ion population during one measurement cycle. Researchers choose a precursor ion according to its mass-to-charge ratio, isolate it from other ions, activate that population, and then record the product ions. Keeping these stages in the same analyzer directly connects selection with fragmentation.
Controlled activation is the key transformation step in this strategy. It converts the isolated precursor population into fragments, which are then measured as product ions. Because activation follows mass-to-charge selection, the observed spectrum can be attributed to the chosen precursor rather than to an unselected mixture. This sequence makes the fragmentation evidence useful for structural elucidation and compound identification.
Connecting a precursor with its product ions creates a more specific molecular signature than precursor-ion measurement alone. The selected mass-to-charge value identifies the ion being examined, while its fragments provide additional structural information. This paired evidence helps researchers distinguish closely related compounds and supports more confident interpretation of chemical measurements.
Mass-to-charge selection defines which precursor contributes to the subsequent fragment pattern. Product-ion signals can therefore be interpreted in relation to a known starting ion instead of being viewed as an undifferentiated collection from the sample. This relationship is especially valuable when chemical mixtures contain multiple compounds with similar characteristics or closely related structures.
A typical workflow begins by selecting a precursor ion with a chosen mass-to-charge ratio in the ion trap. The selected ions are then isolated and subjected to controlled activation, producing fragments. Finally, the analyzer measures the resulting product-ion spectrum. Interpreting that spectrum alongside the selected precursor provides information for molecular characterization and compound identification.
Researchers use Tandem In Time when they need structural information in addition to precursor-ion measurement, particularly for compound identification or analysis of complex chemical mixtures. The approach is relevant to proteomics, metabolomics, and pharmaceutical research, where linking selected ions to their fragments can improve molecular specificity and help separate closely related chemical components.
The product-ion spectrum provides fragment-level evidence about the selected molecule, allowing researchers to investigate its structure and support its identification. In complex samples, this evidence helps associate spectral features with particular precursor ions rather than with the mixture as a whole. Such results make the strategy useful for detailed molecular characterization across several areas of chemistry.