2.00 credits
20.0 h
Q1
Teacher(s)
Morsomme Pierre; Soumillion Patrice;
Language
French
Main themes
The course will be divided into two parts:1. Structural biochemistry:- patterns and forms in protein structures (observation, manipulation, description, classification)- principles of protein folding - domains and assemblies (modular nature of proteins, multi-protein complexes)- bioinformatics in structural biology- interactions between biomolecules (methods and characterization)2. Enzymology- principles of enzyme catalysis (Michaelis Menten, steady state kinetics, reaction schemes)- the basics of chemical catalysis by proteins (catalysis by amino acids lateral chains, active site complementarity, entropic catalysis, transition state stabilisation)- control of enzyme activity (inhibition, activation, cooperativity, allosterism, environmental effects)
Content
About 36 hours will be dedicated to lectures with the help of PowerPoint slides. 6 hours will be organized in computer room for exercises or guided tours of various websites. The course is composed of three main chapters:
Chapter 1. Amino acids side chains: - hydrophobicity/hydrophilicity - electrostatic and acido-basic properties - nucleophilicity - redox properties. Structural biochemistry: - biomolecule structures and interactions: non covalent driving forces and quantitative aspects - thermodynamical and chemical stability of proteins - protein folding : from molecular mechanisms to conformational diseases - observation, manipulation, visualisation, description and classification of three-dimensional structures (in computer room)
Chapter 2: structural biology of membrane proteins
Chapter 3. Enzymology - principles of enzyme catalysis (Michaelis Menten, steady state kinetics, reaction schemes) - the basics of chemical catalysis by proteins (catalysis by amino acids lateral chains, active site complementarity, entropic catalysis, transition state stabilisation) - cofactors and coenzymes chemistries - control of enzyme activity (inhibition, activation, cooperativity, allosterism, environmental effects) - numerical simulation of enzymatic catalysis (in computer room)
Chapter 1. Amino acids side chains: - hydrophobicity/hydrophilicity - electrostatic and acido-basic properties - nucleophilicity - redox properties. Structural biochemistry: - biomolecule structures and interactions: non covalent driving forces and quantitative aspects - thermodynamical and chemical stability of proteins - protein folding : from molecular mechanisms to conformational diseases - observation, manipulation, visualisation, description and classification of three-dimensional structures (in computer room)
Chapter 2: structural biology of membrane proteins
Chapter 3. Enzymology - principles of enzyme catalysis (Michaelis Menten, steady state kinetics, reaction schemes) - the basics of chemical catalysis by proteins (catalysis by amino acids lateral chains, active site complementarity, entropic catalysis, transition state stabilisation) - cofactors and coenzymes chemistries - control of enzyme activity (inhibition, activation, cooperativity, allosterism, environmental effects) - numerical simulation of enzymatic catalysis (in computer room)
Teaching methods
Ex cathedra lectures
Evaluation methods
The course is divided into three modules. Each module will be evaluated during the course of the quadrimester in the form of a dispensatory test.
A written exam will be organized in session for students who have not passed the tests during the quadrimester.
A written exam will be organized in session for students who have not passed the tests during the quadrimester.
Other information
Precursory courses: Basics in biochemistry (e.g. Elements of biochemistry CHM1271)
Online resources
All documents are available via Moodle
Faculty or entity
BIOL
Programmes / formations proposant cette unité d'enseignement (UE)
Title of the programme
Sigle
Credits
Prerequisites
Learning outcomes
Master [120] in Chemistry and Bioindustries
