2019-2020 / BIOL2019-1

Theoretical chemistry and physics applied to biomoleculs structural analysis

Duration

24h Th, 24h Pr

Number of credits

 Bachelor in bioengineering4 crédits 

Lecturer

Christian Damblon, Loïc Quinton

Coordinator

Christian Damblon

Language(s) of instruction

French language

Organisation and examination

Teaching in the second semester

Schedule

Schedule online

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.
Ultraviolet-visible spectrometry.
Infrared and raman spectrometry.
Nuclear magnetic resonance spectrometry (1H, 13C, 2D).
Mass spectrometry.
Coupled techniques.

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

Theoretical lectures.
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% 
Practicals :30% 
Attendance at practical work is mandatory.

Work placement(s)

Organizational remarks

Contacts

Prof. Christian Damblon Laboratoire de chimie biologique structurale UR MolSys Allée du six Aout 11 - Quartier Agora B4000 -Liège 1 - Belgium Département de chimie Université de Liège tel +32 4 366 3788 C.Damblon@uliege.be


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 loic.quinton@uliege.be  

Items online

Sectroscopic methods, Mass Spectrometry
Molecular structure analysis, mass spectrometry