Lecture

Protein Structure Exploration

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In course

CH-210: Biochemistry

Les constituants biochimiques de l'organisme, protéines, glucides, lipides, à la lumière de l'évolution des concepts et des progrès en biologie moléculaire et génétique, sont étudiés. ...

Description

This lecture covers the composition, synthesis, and exploration of proteins, including protein purification methods such as affinity chromatography and gel-filtration chromatography. It also delves into techniques like mass spectrometry, electrophoresis, and protein sequencing. The instructor explains how proteins are extracted from cells, separated, and analyzed to understand their structure and function.

Instructor

Christian Heinis

Teaching & PhD PhD Students Thomas Julien Denis Emel, Alessandro Scapozza, Nathan Moïse De Sadeleer, Florian Handel, Hugo André Clerc, Frédéric Brantschen, Grégoire Menoud, Ines Michrafy, Jonathan Schmitt, Laura Elena Massaad Past EPFL PhD Students Jeremy Touati, Shiyu Chen, Sophie Venet-Bonnot, Lisa Pollaro, Inmaculada Rentero Rebollo, Philippe Diderich, Charlotte Urech-Varenne, Silvia Bellotto, Davide Bertoldo, Alessandro Zorzi, Camille Villequey, Jonas Alfred Karl Wilbs, Grigory Karateev, Vanessa Carle

Official source

Related concepts (32)

Protein structure

Protein structure is the three-dimensional arrangement of atoms in an amino acid-chain molecule. Proteins are polymers - specifically polypeptides - formed from sequences of amino acids, which are the monomers of the polymer. A single amino acid monomer may also be called a residue, which indicates a repeating unit of a polymer. Proteins form by amino acids undergoing condensation reactions, in which the amino acids lose one water molecule per reaction in order to attach to one another with a peptide bond.

Gel electrophoresis

Gel electrophoresis is a method for separation and analysis of biomacromolecules (DNA, RNA, proteins, etc.) and their fragments, based on their size and charge. It is used in clinical chemistry to separate proteins by charge or size (IEF agarose, essentially size independent) and in biochemistry and molecular biology to separate a mixed population of DNA and RNA fragments by length, to estimate the size of DNA and RNA fragments or to separate proteins by charge.

Protein biosynthesis

Protein biosynthesis (or protein synthesis) is a core biological process, occurring inside cells, balancing the loss of cellular proteins (via degradation or export) through the production of new proteins. Proteins perform a number of critical functions as enzymes, structural proteins or hormones. Protein synthesis is a very similar process for both prokaryotes and eukaryotes but there are some distinct differences. Protein synthesis can be divided broadly into two phases—transcription and translation.

Chromatography

In chemical analysis, chromatography is a laboratory technique for the separation of a mixture into its components. The mixture is dissolved in a fluid solvent (gas or liquid) called the mobile phase, which carries it through a system (a column, a capillary tube, a plate, or a sheet) on which a material called the stationary phase is fixed. Because the different constituents of the mixture tend to have different affinities for the stationary phase and are retained for different lengths of time depending on their interactions with its surface sites, the constituents travel at different apparent velocities in the mobile fluid, causing them to separate.

Protein folding

Protein folding is the physical process where a protein chain is translated into its native three-dimensional structure, typically a "folded" conformation, by which the protein becomes biologically functional. Via an expeditious and reproducible process, a polypeptide folds into its characteristic three-dimensional structure from a random coil. Each protein exists first as an unfolded polypeptide or random coil after being translated from a sequence of mRNA into a linear chain of amino acids.

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