Suspension Trapping
Suspension Trapping - Related Videos
01:41
Social Traps
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2020
Social traps are negative situations where people get caught in a direction or relationship that later proves to be unpleasant, with no easy way to back out of or avoid. The concept was orignally introduced by John Platt who applied psychology to Garrett Hardin's "Tragedy of the Commons", where in New England herd owners could let their cattle graze in the common ground. This situation seems like a good idea, but an individual could have an advantage. If they owned more cows, the larger...
11:45
Experimental Methods for Trapping Ions Using Microfabricated Surface Ion Traps
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Cited by 19 •
2017
This paper presents a microfabrication methodology for surface ion traps, as well as a detailed experimental procedure for trapping ytterbium ions in a room-temperature environment.
08:20
A Protein Suspension-Trapping Sample Preparation for Tear Proteomics by Liquid Chromatography-Tandem Mass Spectrometry
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Cited by 2 •
2023
This protocol describes a method for collecting tear samples using Schirmer strips and an integrated quantitative workflow for discovering non-invasive tear protein biomarkers. The suspension trapping sample preparation workflow enables fast and robust tear sample preparation and mass spectrometric analysis, resulting in higher peptide recovery yields and protein identification than standard in-solution procedures.
13:39
Optical Trapping of Nanoparticles
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Cited by 7 •
2013
The following setup approach details low power optical trapping of dielectric nanoparticles using a double-nanohole in metal film.
05:57
Dean-Stark Trap
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2023
Source: Vy M. Dong and Jan Riedel, Department of Chemistry, University of California, Irvine, CA A Dean-Stark trap is a special piece of glassware, which allows the collection of water during a reaction through an azeotropic distillation. The desire to collect water from a reaction can have various reasons. It can drive the equilibria in reactions, where water is formed as a byproduct. According to Le Chatelier's principle, a change in temperature, pressure, concentration, or volume will cause...
FAQs
Acidification and methanol transform proteins in a complex lysate into a particulate suspension. This physical change allows the material to become immobilized within the porous quartz filter rather than remaining freely dissolved. The resulting capture step separates the protein-containing particulate material from components that can pass through the filter, supporting subsequent enzymatic processing.
The porous quartz filter provides the physical structure that retains the protein suspension after it forms. Proteins remain immobilized inside the filter, while detergents such as SDS pass through. This selective behavior is important because it prepares the trapped protein material for digestion without carrying the detergent into later peptide recovery and analysis steps.
Removing SDS during trapping helps create conditions in which trypsin can digest the immobilized proteins efficiently. The proteins are converted into peptides within the workflow, and the absence of detergent supports their recovery for downstream liquid chromatography–mass spectrometry. As a result, the preparation can improve digestion efficiency and contribute to reproducible protein identification and quantitative analysis.
The workflow begins with a complex biological lysate, followed by acidification and methanol addition to produce a particulate protein suspension. That suspension is immobilized in a porous quartz filter while SDS passes through. Trypsin then digests the trapped proteins into peptides, which are recovered by elution for liquid chromatography–mass spectrometry.
Suspension trapping can be applied to protein samples derived from cells, tissues, and other biological materials. Its value is especially relevant when lysates contain complex mixtures and detergents that must be handled before proteolysis. Preparing these materials through the same trapping and elution sequence supports protein identification and quantitative analysis across varied biochemical sample sources.
After digestion and peptide elution, the prepared material can be analyzed by liquid chromatography–mass spectrometry. This supports identification of proteins present in the original biological material and enables quantitative analysis. The workflow is also associated with improved proteolytic digestion and reproducible sample preparation, making it useful in biochemical and proteomic studies of complex lysates.