6 ECTS credits
156 h study time
Offer 1 with catalog number 1010277BNR for all students in the 2nd semester at a (B) Bachelor - advanced level.
This class covers a series of biophysical techniques that are used to investigate different aspects of the three-dimensional structure of organic molecules and biological macromolecules (proteins, DNA, RNA). Topics that are being dealt with include X-ray diffraction, with special emphasis on single-crystal diffraction, nuclear magnetic resonance, mass spectrometry and classical spectroscopies, including UV absorption, fluorescence, circular dichroism, infrared and Raman spectroscopy and light scattering.
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. During the practical sessions the techniques will be further illustrated. This will be achieved through a combination of hands-on experiments (crystallization of a protein) and demonstrations (X-ray data collection, CD, UV and fluorescence spectroscopy), complemented with the structural analysis of a protein on the computer.
Presence during te practicals is obligatory. The evaluation of the practical session in second terms is not possible.
Unjustified absence on the practical sessions leads to substraction of 1 point on the global exam result, per missed practical session. Unjustified absence on more than half of the practical sessions leads to exclusion from participation to the exam.
- The students have profound knowledge about and have insight in the theory of X-ray diffraction
- The students have profound knowledge about and have insight in the theory of nuclear magnetic resonance and know how to interpret simple NMR spectra
- The students understand how three-dimensional structures of macromolecules can be determined using X-ray diffraction or NMR
- The students have obtained knowledge and insight into the different methods used for mass spectrometry.
- The students are knowledgeable on the different spectroscopic methods used in biochemistry (UV absorption, UV fluorescence, circular dichroism, infrared and Raman spectroscopy, light scatter) and can apply this knowledge to a simple practical case in biochemistry
- The students have insight into the advantages and disadvantages of the different techniques used in structure determination
- The students posses practical skills with regard to spectroscopic analysis and crystallization of macromolecules, and can interpret diffraction patterns and electron density maps.
The final grade is composed based on the following categories:
Written Exam determines 100% of the final mark.
Within the Written Exam category, the following assignments need to be completed:
Written exam (closed books). The students will be presented with a number of questions that cover the different topics of the course: part 1: X-ray diffraction, part 2: NMR, and part 3: spectroscopy and mass spectrometry. Both knowledge and insights in these topics will be tested.
These three parts will obtain an identical weight in the calculation of the final grade.
Practical skills will evaluated formatively during the practical session and can be touched upon during the written exam. Presence and active participation in the practicals is compulsory. Unjustified absence on the practical sessions leads to substraction of 1 point on the global exam result, per missed practical session. Unjustified absence on more than half of the practical sessions leads to exclusion from participation to the exam.
This offer is part of the following study plans:
Bachelor of Chemistry: Default track (only offered in Dutch)