Lecture

Proteomics and Mass Spectrometry

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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 principles and techniques of protein mass spectrometry and proteomics, focusing on bottom-up and top-down strategies, sample preparation, and separation techniques like gel electrophoresis and liquid chromatography. It also discusses quantitative workflows, bioinformatics tools, and applications in biology and clinical research.

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.

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.

Protein microarray

A protein microarray (or protein chip) is a high-throughput method used to track the interactions and activities of proteins, and to determine their function, and determining function on a large scale. Its main advantage lies in the fact that large numbers of proteins can be tracked in parallel. The chip consists of a support surface such as a glass slide, nitrocellulose membrane, bead, or microtitre plate, to which an array of capture proteins is bound. Probe molecules, typically labeled with a fluorescent dye, are added to the array.

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.

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).

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