3 ECTS credits
78 h study time
Offer 1 with catalog number 4021486ENR for all students in the 1st semester at a (E) Master - advanced level.
Proteins are the most versatile and dynamic macromolecules in living systems and serve crucial functions in essentially all biological processes. They are linear polymers built of amino acids. Remarkably, proteins spontaneously fold into precise three-dimensional structures that are determined by the sequence of amino acids in the linear polymer. Proteins contain a wide range of chemically reactive functional groups, which accounts for a broad spectrum of functions.
This course blends scientific background information on proteins and protein biochemistry with the methods and techniques to study them. The course intends to give the student self confidence in being able to understand the way proteins behave and the basis of the methods used to separate, identify, and characterize them.
We will study
-key concepts of magnitude of quantities, units, dilutions, UV-absorbance measurements, acids/bases and buffers
-Properties of proteins and how to explore them
-Determination of protein concentration
-Molecular mass determination
-Separation of proteins
-Purification of proteins
-Analysis of protein purity
-key concepts of enzyme assays
-key concepts of binding assays
After every theoretical part, students will be performing exercises on the black boards and in small groups in the class room. Students will be trained on recognition of a problem and the use of the correct flowchart to solve a problem. Through intense interactions with the students, I find out what the general fundamental misconceptions are, and those are being discussed in detail in front of the class.
Therefore, it is a prerequisite that this course can be taught in a class room which is big enough to accommodate all the students to sit in working groups, and with plenty of blackboards on the walls.
Power point slides containing the course material and specific course notes will be made available via the learning platform.
Course material
The student can evaluate and analyse a new problem and apply the specific knowledge to solve a problem. Specifically, the student can
-convert dimensions
-calculate dilutions, and equilibrium constants
-calculate the molar and 0.1% extinction coefficient of a polypeptide and the concentration using the law of Lambert-Beer
-calculate steady-state enzymatic parameters and inhibition constants
-calculate dissociation and affinity constants
-can write the correct sequence of a polypeptide chain starting from the one letter code at several pHs, can calculate the pI, and the charge of the polypeptide chain along a titration curve
-design a strategy to purify a protein
At the end of the course, the student should be able to make relationships and connections between the several topics discussed. This requires a deep, thorough, and profound understanding of
-pKa, pKb, the Henderson-Hasselbalch equation, and buffering against pH changes in biological systems
-structure of water, amino acids, polypeptide chain
-enzymes (catalysis, Michaelis Menten and Lineweaver-Burk plot, reversible inhibition)
-weak interactions used by proteins and how these interactions are being used in several methods to purify and analyse proteins
The final grade is composed based on the following categories:
Other Exam determines 100% of the final mark.
Within the Other Exam category, the following assignments need to be completed:
Written preparation of general questions that relate to different parts of the course combined with integrated exercises, which tests the deep and thorough understanding of the course material.
This offer is part of the following study plans:
Master of Molecular Biology: Standaard traject
Master of Biology: Molecular and Cellular Life sciences