Lecture

Chemistry of Amino Acids

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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 introduces the organization of the course, including weekly exercises and discussion sessions. It covers the composition and structure of proteins, protein synthesis, and the exploration of genes and genomes. The lecture delves into the ionization state of amino acids, the strengths of molecular interactions, and the classes of biomolecules. It explains the significance of pH, the state of ionization of functional groups, and the role of side chains in protein structure. The session also discusses the formation of disulfide bridges and the primary structure of proteins.

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 primary structure

Protein primary structure is the linear sequence of amino acids in a peptide or protein. By convention, the primary structure of a protein is reported starting from the amino-terminal (N) end to the carboxyl-terminal (C) end. Protein biosynthesis is most commonly performed by ribosomes in cells. Peptides can also be synthesized in the laboratory. Protein primary structures can be directly sequenced, or inferred from DNA sequencess.

Biomolecular structure

Biomolecular structure is the intricate folded, three-dimensional shape that is formed by a molecule of protein, DNA, or RNA, and that is important to its function. The structure of these molecules may be considered at any of several length scales ranging from the level of individual atoms to the relationships among entire protein subunits. This useful distinction among scales is often expressed as a decomposition of molecular structure into four levels: primary, secondary, tertiary, and quaternary.

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.

Essential amino acid

An essential amino acid, or indispensable amino acid, is an amino acid that cannot be synthesized from scratch by the organism fast enough to supply its demand, and must therefore come from the diet. Of the 21 amino acids common to all life forms, the nine amino acids humans cannot synthesize are valine, isoleucine, leucine, methionine, phenylalanine, tryptophan, threonine, histidine, and lysine.

Genome

In the fields of molecular biology and genetics, a genome is all the genetic information of an organism. It consists of nucleotide sequences of DNA (or RNA in RNA viruses). The nuclear genome includes protein-coding genes and non-coding genes, other functional regions of the genome such as regulatory sequences (see non-coding DNA), and often a substantial fraction of junk DNA with no evident function. Almost all eukaryotes have mitochondria and a small mitochondrial genome.

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