Lecture

Proteomics and Mass Spectrometry

Graph Chat

Chat with Graph Search

Ask any question about EPFL courses, lectures, exercises, research, news, etc. or try the example questions below.

DISCLAIMER: The Graph Chatbot is not programmed to provide explicit or categorical answers to your questions. Rather, it transforms your questions into API requests that are distributed across the various IT services officially administered by EPFL. Its purpose is solely to collect and recommend relevant references to content that you can explore to help you answer your questions.

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 gel electrophoresis, isoelectric focusing, and liquid chromatography. It explains the importance of protein separation, sampling, and preparation, highlighting the need for separation due to the diversity of protein sequences and concentrations. The lecture also discusses the use of tandem mass spectrometry for protein identification and the generation of tandem mass spectra. Various electrophoresis set-ups, polyacrylamide gel polymerization, and 1D SDS PAGE techniques are explained in detail, along with the properties of amino acids and their role in isoelectric focusing. The lecture concludes with a discussion on the charge of polypeptides and the generation of pH gradients for protein separation.

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

Related concepts (32)

Agarose gel electrophoresis

Agarose gel electrophoresis is a method of gel electrophoresis used in biochemistry, molecular biology, genetics, and clinical chemistry to separate a mixed population of macromolecules such as DNA or proteins in a matrix of agarose, one of the two main components of agar. The proteins may be separated by charge and/or size (isoelectric focusing agarose electrophoresis is essentially size independent), and the DNA and RNA fragments by length.

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.

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).

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.

Related lectures (64)

Protein Mass Spectrometry and Proteomics

Explores protein mass spectrometry, chromatographic techniques, and quantitative proteomic workflows, including SILAC and isobaric tagging methods.

Exploring Proteins: Structure, Purification, and Analysis

Covers protein exploration, purification, and analysis methods, including sequencing, concentration measurement, and antibody detection.

Proteomics and Mass Spectrometry

Covers the basics of proteomics, mass spectrometry, protein synthesis, and amino acids, emphasizing the importance of molecular weight and isotopic abundance.

Proteomics: Steps and Protein Digestion Techniques

Provides an overview of the key steps in proteomics, focusing on protein digestion and the techniques used for analysis.

Mass Spectrometry Fundamentals