24h Th, 24h Pr
Number of credits
|Bachelor in bioengineering||4 crédits|
Language(s) of instruction
Organisation and examination
Teaching in the second semester
Units courses prerequisite and corequisite
Prerequisite or corequisite units are presented within each program
Learning unit contents
Description of the ralation between the different spectrometries.
Quantic theory and Schrödinger equation.
Infrared and raman spectrometry.
Nuclear magnetic resonance spectrometry (1H, 13C, 2D).
Learning outcomes of the learning unit
Understand theoretical basis of spectrometric methods. Apply these techniques to structural analysis of biological molécules. After completing the course the student is expected to - understand phenomenons that govern the different spectrometry : ultra-violet, visible, infrared, raman, nuclear magnetic resonance, mass spectrometry. - read and explain spectra obtained by the different techniques - apply these techniques on corresponding instruments - identify a molecule from its different spectra
Prerequisite knowledge and skills
CHIM9268-1 - General Chemistry CHIM9255-3 - Organic Chemistry CHIM9239-2 - Biological molecules chemistry CHIM9267-1 - Equilibrium Chemistry
Planned learning activities and teaching methods
Interpretation exercises of spectra obtained by different spectrometers. The exercises include a brief theoretical reminder with interpretation of the spectra of different chemical functions, spectrometry exercises made by students with the help of the teacher, summary exercises implementing different spectra for the same unknown molecule.
Practical work for techniques of IR, MALDI-TOF, LC-MS, GC-MS and NMR. Practical work are given by sets of students working in groups. The experiments illustrate and complement the theoretical notions. Writing a report is requested at the end of the sessions. The presence in the laboratory is mandatory. Any absence must be justified by a medical certificate in proper form. Access to the exam will not be granted to students who have unjustified absences from the TPs or who have not submitted a TP report. For security reasons, access to the laboratory is authorized only for Students with a lab coat, their safety glasses and in order of registration. Glasses should be worn when handling. There is no practical work examination as such. However, questions involving laboratory situations and laboratory 'vocabulary' may appear when evaluating for exercises.
Mode of delivery (face-to-face ; distance-learning)
Lectures : 24h Practical Works : 24h (Execises 8h, practical work on devices 16h)
Recommended or required readings
The course notes include some of the literature that refers student to books that can help to better understanding of the material.
Assessment methods and criteria
Students must bring their student Ulg card and their identity card to attend all events, under penalty of being denied access and consideration of the event.
The distribution of evaluations is as follows:
- Written exam:Theory + exercices: 70%
Attendance at practical work is mandatory.
Prof. Christian Damblon
Laboratoire de chimie biologique structurale
Allée du six Aout 11 - Quartier Agora
B4000 -Liège 1 - Belgium
Département de chimie
Université de Liège
tel +32 4 366 3788
Prof. Loïc Quinton Laboratory of Mass Spectrometry - Biological Chemistry MolSys Research Unit Allée du six Aout 11 - Quartier Agora B4000 -Liège 1 - Belgium Tel +32 4 366 3679 firstname.lastname@example.org
Sectroscopic methods, Mass Spectrometry
Molecular structure analysis, mass spectrometry