Distinguishing between Phosphorylated and Nonphosphorylated Peptides by Ion Mobility−Mass Spectrometry (CAT#: STEM-ST-0148-LJX)

Introduction

Mass spectrometry has become an indispensable tool in identifying post-translationally modified proteins, but multiple peptide mass-mapping/peptide-sequencing experiments are required to answer questions involving the site and type of modification present. Here, we apply ion mobility−mass spectrometry (IM−MS), a high-throughput analysis method having high selectivity and sensitivity, to the challenge of identifying phosphorylated peptides. Ion mobility separation is based on the collision cross-section of the ion. Phosphorylation can result in a conformational change in gas-phase peptide ions, which can be detected by IM.

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Principle Applications Procedure Materials Notes Related Products

Principle

Ion mobility spectrometry–mass spectrometry (IMS-MS) is an analytical chemistry method that separates gas phase ions based on their interaction with a collision gas and their masses. In the first step, the ions are separated according to their mobility through a buffer gas on a millisecond timescale using an ion mobility spectrometer. The separated ions are then introduced into a mass analyzer in a second step where their mass-to-charge ratios can be determined on a microsecond timescale.

Applications

For studying the gas phase ion structure
For detecting the chemical warfare agents and explosives
For the analysis of proteins, peptides, drug-like molecules and nano particles
For monitoring isomeric reaction intermediates and probe their kinetics
For proteomics and pharmaceutical analysis

Procedure

1. Add sample
2. The ions in the sample are separated in the ion mobility spectrometer
3. The separated ions are introduced into the mass analyzer for detection
4. Store the detection results

Materials

• Sample Type:
Peptides

Notes

1. Ion mobility spectrometry is also a very fast technique, making it suitable for high-throughput applications. The entire analysis can be completed in just a few minutes.
2. The method is extremely sensitive and able to detect trace amounts of contaminants that other spectrometry methods would miss.
3. The effective separation of analytes achieved with this method makes it widely applicable in the analysis of complex samples such as in proteomics and metabolomics.

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