3 ECTS credits
75 h study time
Offer 1 with catalog number 4021497ENR for all students in the 1st semester at a (E) Master - advanced level.
This class covers a number of theoretical concepts dealing with the functionality of proteins as well as some of the biophysical techniques that are used to investigate different aspects of the three-dimensional structure of organic molecules and biological macromolecules (proteins, DNA, RNA).
The class consists of two major parts. Part 1 deals with biological spectroscopy and introduces different spectroscopic methods that are used in molecular and cellular biophysics: UV absorption, fluorescence, circular dichroism, Infra red and Raman spectroscopy, light and X-ray scatter, and NMR. During the lectures the theory underlying these methods is introduced and their practical applications are illustrated using a number of examples taken from the literature.
Part 2 deals with the (non-covalent) forces and thermodynamic principles underlying the stability and folding of proteins as well as their interaction with ligands. The principles behind commonly used methods to study the stability and folding pathways of proteins are introduced. Finally, the kinetics and thermodynamics of protein-ligand interactions are discussed. Common binding models and methods to derive binding parameters (e.g. isothermal titration calorimetry and surface plasmon resonance) are dealt with.
Power point slides containing the course material and specific course notes on spectroscopy are made available via the on-line learning platform.
- The student knows and understands the principles behind the different spectroscopic methods used in biochemistry (UV absorption, UV fluorescence, circular dichroism, infrared and Raman spectroscopy, light scatter).
- The students knows the information that can be obtained from these different spectroscopic methods and can apply this knowledge to a simple practical case in biochemistry.
- The student has a basic knowledge of the types of experiments that lead to structural models of macromolecules
- The student understands the basics of protein structure and knows and understand the levels of structural detail that are obtained from different techniques including NMR, X-ray crystallography, SAXS, electron microscopy and homology modelling.
- The student knows and understands the non-covalent interactions that contribute to protein folding and ligand binding in an aqueous environment.
- The student knows and understands the physico-chemical principles that determine protein stability and folding and know the experimental methods to determine these.
- The student has knowledge of and insight in the principles of ligand binding, the most common binding models and a number of important methods to study ligand binding and derive the relevant parameters (K-D, k-on and k-off)
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:
The evaluation consists of a written exam. The students receive several open questions that cover te entire course. The questions will probe both knowledge and insight and may be formulated in the form of a small problem. Questions may relate to (part of) a specific chapter or may link two or more chapters. Basic knowledge of biochemistry (e.g. structure formula of the 20 amino acids and of the DNA and RNA nucleotides, the concept of pKa, ...) is assumed and may be required to answer some exam questions.
This offer is part of the following study plans:
Master of Molecular Biology: Standaard traject