Lecture

Protein Mass Spectrometry and Proteomics

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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 fundamentals of protein mass spectrometry and proteomics, including the introduction to protein analysis, mass spectrometry reminders, ionization sources, analyzers, and detectors used in proteomics. It also delves into proteomic strategies, workflows, separations techniques, quantitative proteomic workflows, proteomic bioinformatics, and applications to biology and clinical research. The content includes discussions on bottom-up proteomics, peptide mass fingerprinting, protein identification using MS/MS data, and the comparison between PMF and MS/MS ion search methods.

Instructor

Loïc Dayon

Teaching & PhD Courses Protein mass spectrometry and proteomics CH-419 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 via mass spectrometry.

Official source

Ontological neighbourhood

Chemistry

Analytical chemistry: Mass spectrometry

Related concepts (32)

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.

Protein sequencing

Protein sequencing is the practical process of determining the amino acid sequence of all or part of a protein or peptide. This may serve to identify the protein or characterize its post-translational modifications. Typically, partial sequencing of a protein provides sufficient information (one or more sequence tags) to identify it with reference to databases of protein sequences derived from the conceptual translation of genes. The two major direct methods of protein sequencing are mass spectrometry and Edman degradation using a protein sequenator (sequencer).

Ion source

An ion source is a device that creates atomic and molecular ions. Ion sources are used to form ions for mass spectrometers, optical emission spectrometers, particle accelerators, ion implanters and ion engines. Electron ionization Electron ionization is widely used in mass spectrometry, particularly for organic molecules. The gas phase reaction producing electron ionization is M{} + e^- -> M^{+\bullet}{} + 2e^- where M is the atom or molecule being ionized, e^- is the electron, and M^{+\bullet} is the resulting ion.

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.

Electron ionization

Electron ionization (EI, formerly known as electron impact ionization and electron bombardment ionization) is an ionization method in which energetic electrons interact with solid or gas phase atoms or molecules to produce ions. EI was one of the first ionization techniques developed for mass spectrometry. However, this method is still a popular ionization technique. This technique is considered a hard (high fragmentation) ionization method, since it uses highly energetic electrons to produce ions.

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Related concepts (32)

Proteomics

Protein sequencing

Ion source

Liquid chromatography–mass spectrometry

Electron ionization