cookieImage
2026-2027 / BIOC9243-1

Equilibria in biochemistry and enzime kinetics

Duration

20h Th, 40h Pr

Number of credits

 Bachelor in biology4 crédits 
 Master of education, Section 4: Biology4 crédits 

Lecturer

André Matagne

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

The first part of this course highlights the importance of equilibria in biochemistry and covers the following topics: (1) chemical equilibria; (2) acid-base equilibria; (3) complexation equilibria. The second part introduces fundamental concepts in enzymology and enzyme kinetics: (1) general properties of enzymes; (2) steady-state enzyme kinetics; (3) enzyme inhibition. The topics are explored in greater depth in the master's-lecel course entitled "Biotechnologies".

Learning outcomes of the learning unit

By the end of this course, students will have acquired the fundamental concepts required to study equilibria in biochemistry and enzyme kinetics. They will understand the essential principles of enzyme function and be able to use the main tools employed for their kinetic characterization.

Prerequisite knowledge and skills

Basic knowledge of mathematics, chemistry and biochemistry.

Planned learning activities and teaching methods

The first part of the course, delivered through lectures, focuses on the main factors governing equilibria in biochemistry. The second part provides an introduction to enzyme kinetics. Tutorial sessions and practical laboratory work allow students to apply the concepts acquired during the course to concrete situations.

Attendance at the preparatory session and all practical laboratory sessions is compulsory.

Mode of delivery (face to face, distance learning, hybrid learning)

Face-to-face course


Further information:

Teaching is conducted entirely in person. Most lectures are delivered using the blackboard and white chalk. Tutorial sessions are also organized to allow students to solve practical problems related to selected theoretical topics. Finally, 40 hours of laboratory work are devoted to enzyme kinetics.

Attendance at the introductory laboratory session is mandatory and is a prerequisite for participation in the subsequent practical sessions.

 

Course materials and recommended or required readings

Platform(s) used for course materials:
- MyULiège


Further information:

Lecture notes are provided progressively as the course advances. They are intended to facilitate the study of the course material, but their use is not compulsory to acquire the learning outcomes of this course.
 

Recommended reference books:

N.C. Price, R.A. Dwek, R.G. Ratcliffe and M.R. Wormald, Principles and Problems in Physical Chemistry for Biochemists, Third Edition, Oxford University Press, 2001.

K.E. van Holde, W. C. Johnson, P.S. Ho, Principles of Physical Biochemistry, Prentice Hall, 1998.

A. Cornish-Bowden, M. Jamin, V. Saks: Cinétique enzymatique, Grenoble Sciences/EDP Sciences, 2005.

A.R. Fersht, Structure and mechanism in protein science, W.H. Freeman and Co, 1999.



 

Exam(s) in session

Any session

- In-person

written exam ( open-ended questions )

Written work / report


Further information:

Assessment is based on a written examination, which accounts for 70% of the final grade, and on the work carried out during the practical sessions and the activity report, which together account for 30% of the final grade.

Active, in-person participation in all practical sessions is compulsory. In accordance with Article 61 of the General Study and Examination Regulations, students who fail to meet this requirement will not be allowed to take the assessments organized for this course unit or to obtain the corresponding credits.

Work placement(s)

Non applicable

Organisational remarks and main changes to the course

Classes are held according to the schedule communicated to the students, unless otherwise indicated. Students will be informed in advance of any change to the schedule, including the cancellation of a session, either during class or by email, where appropriate through the class representative.

Contacts

André Matagne, PhD, Full Professor, Enzymology and Protein Folding, Centre for Protein Engineering, InBioS RU, Life Science Department, Institut de Chimie B6c (room 3/1), Allée de la Chimie, 3, University of Liège, B4000 Liège (Sart-Tilman), Tel.: +32 (0)4 3663419, Email: amatagne@uliege.be (to be preferred)

Association of one or more MOOCs