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En pratique :

Volume horaire de cours : 16
Volume horaire global de TD : 23
Volume horaire global de TP : 9
Volume horaire pour d'autres type d'enseignement : 2
Langue principale : Anglais
Nombre de crédits européens : 5

Description du contenu de l'enseignement

Teaching program:
Lecture Contents:

  • Monosaccharides, oligosaccharides and polysaccharides: glucose, mannose, galactose, sucrose, lactose, starches and glycogen.
  • Amino acid’s structures and properties
  • Lipids structures and properties: acylglycerols, glycerophospholipids, cholesterol and its derivatives.
  • Nucleotides and nucleic acids.

Tutorial work

Classes are a mix of lectures and tutorials allowing enforcement of the concept immediately with exercises. The objective is to write molecules and work on structure-functions in accordance with experimental results.

Practical work

Students will perform colorimetric assays in 3 practical sessions:

  • Phenolphthalein concentration determination,
  • Egg yolk lipid analysis and determination of cholesterol level,
  • Separation of 2 amino acids by ion exchange chromatography and colorimetric assay of arginine.

Compétences à acquérir

Teaching description

To introduce saccharides, oligosaccharides and polysaccharides. To describe isomerism of saccharides. To be able to represent structures of glucose and other hexoses according to Fisher and Haworth representations. To draw structures of the main disaccharides and polysaccharides.
To specify structures of saturated and unsaturated fatty acids and to explain how the length of the chain and its level of unsaturation influence the melting temperature. To draw the general structure of triacylglycerols, phospholipids, cholesterol and its derivatives. To understand the behaviour of lipids in aqueous and organic media.
To know names, structures and 3 letters code of amino acids present in proteins. To identify ionisable functions and to assign a pKa value. To be able to calculate the pH of an amino acid buffered solution. To represent a peptide bond. To draw an oligopeptide, to calculate its pHi and to predict its electrophoretic mobility. To reconstitute a peptidic sequence from results of chemical or enzymatic treatments.
To draw puric and pyrimidic bases. To draw the main nucleotides of DNA and RNA. To draw a polynucleotide. To understand the 5’-3’ orientation of phosphodiester bonds. To represent base pairing. To explain hyperchromicity.
To follow a lab class protocol. To prepare a colorimetric assay protocol. To calculate a dilution factor in order to assay a solution having an unknown concentration with a fixed standard range.

Learning outcomes:
At the end of this course the student must:

  • Be able to draw biomolecules’ structures.
  • Know biomolecules essential properties and characteristics.
  • Be able to use simple qualitative analysis techniques.
  • Identify and perform in autonomy the different steps of a colorimetric assay
  • Be acquainted with basic molar and mass calculations.

Modalités pédagogiques

  • hybride
  • en présence