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Lecture

Protein Mass Spectrometry and Proteomics

In course

CH-419: Protein mass spectrometry and proteomics

In systems biology, proteomics represents an essential pillar. The understanding of protein function and regulation provides key information to decipher the complexity of living systems. Proteomic technology now enables deep quantitative proteome mapping v ...

Description

This lecture covers the principles and techniques of protein mass spectrometry and proteomics, including protein identification using MS/MS data, direct analysis of complex protein mixtures, liquid chromatography tandem mass spectrometry, data-dependent acquisition, top-down and middle-down proteomics, sample preparation, reduction and alkylation, protein digestion, and depletion and enrichment strategies. It discusses the challenges and applications of top-down proteomics, the importance of high resolution mass spectrometry, and the use of native mass spectrometry. The lecture also addresses the significance of data analysis, the role of native mass spectrometry in disease mechanisms, and the assessment of post-translational modifications and sequence variations.

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Instructor

Loïc Dayon

Official source

Ontological neighbourhood

Chemistry

Analytical chemistry: Mass spectrometry

Related concepts (32)

Tandem mass spectrometry

Tandem mass spectrometry, also known as MS/MS or MS2, is a technique in instrumental analysis where two or more mass analyzers are coupled together using an additional reaction step to increase their abilities to analyse chemical samples. A common use of tandem MS is the analysis of biomolecules, such as proteins and peptides. The molecules of a given sample are ionized and the first spectrometer (designated MS1) separates these ions by their mass-to-charge ratio (often given as m/z or m/Q).

Mass spectrometry

Mass spectrometry (MS) is an analytical technique that is used to measure the mass-to-charge ratio of ions. The results are presented as a mass spectrum, a plot of intensity as a function of the mass-to-charge ratio. Mass spectrometry is used in many different fields and is applied to pure samples as well as complex mixtures. A mass spectrum is a type of plot of the ion signal as a function of the mass-to-charge ratio.

Liquid chromatography–mass spectrometry

Liquid chromatography–mass spectrometry (LC–MS) is an analytical chemistry technique that combines the physical separation capabilities of liquid chromatography (or HPLC) with the mass analysis capabilities of mass spectrometry (MS). Coupled chromatography - MS systems are popular in chemical analysis because the individual capabilities of each technique are enhanced synergistically. While liquid chromatography separates mixtures with multiple components, mass spectrometry provides spectral information that may help to identify (or confirm the suspected identity of) each separated component.

Proteomics

Proteomics is the large-scale study of proteins. Proteins are vital parts of living organisms, with many functions such as the formation of structural fibers of muscle tissue, enzymatic digestion of food, or synthesis and replication of DNA. In addition, other kinds of proteins include antibodies that protect an organism from infection, and hormones that send important signals throughout the body. The proteome is the entire set of proteins produced or modified by an organism or system.

Ion-mobility spectrometry–mass spectrometry

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.

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Mass Spectrometry: Analyzing Peptides with Tandem MS

Covers mass spectrometry and tandem MS/MS techniques for peptide analysis, focusing on ionization, fragmentation, and sequence identification.

Proteomics Profiling Methods

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Automation in Protein Identification: Techniques and Workflows