Note from June 29, 2020
Although we do not yet know how long the social distancing related to the Covid-19 pandemic will last, and regardless of the changes that had to be made in the evaluation of the June 2020 session in relation to what is provided for in this learning unit description, new learnig unit evaluation methods may still be adopted by the teachers; details of these methods have been - or will be - communicated to the students by the teachers, as soon as possible.
Although we do not yet know how long the social distancing related to the Covid-19 pandemic will last, and regardless of the changes that had to be made in the evaluation of the June 2020 session in relation to what is provided for in this learning unit description, new learnig unit evaluation methods may still be adopted by the teachers; details of these methods have been - or will be - communicated to the students by the teachers, as soon as possible.
2 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 24 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.
Content:
1. Amino acids side chains:
- hydrophobicity/hydrophilicity
- electrostatic and acido-basic properties
- nucleophilicity
- redox properties
2. 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)
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
Written exam
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
Aims
Master [120] in Chemistry and Bioindustries
