5 ECTS credits
150 h study time
Offer 1 with catalog number 4016677ENR 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. All these concepts are illustrated using selected examples.
First the properties of proteins that determine their 3-dimensional structure are described in depth. Starting from the chemical reactivity of the individual amino acids, the non-covalent interactions that determine the 3-dimensional structure are discussed. This leads towards a detailed description of the secondary structures and tertiary motifs that determine the course of the main chain, and of the specific interactions between the side chains that encode the fold. Further attention goes to the importance of the flexibility of proteins in their functionality, including intrinsically unfolded proteins.
A second part covers an in depth description of the stability and folding mechanisms of proteins. Special attention is given to the theoretical principles as well as to the experimental methods.
In a last part a number of important functions of proteins are discussed, including ligand binding and enzyme kinetics and mechanisms.
Handouts accompanying the course will be made available on the learning platform.
- The students have knowledge of the chemical reactivity of amino acids and can interpret these in the context of chemical modification of proteins
- The students know and understand the non-covalent interactions that contribute to protein folding and ligand binding in an aqueous environment
- The students have profound knowledge of and insight into the structure and function of proteins. They know the different (super)secondary structure elements and know by which parameters these are determined. They understand how protein structure evolves in function of amino acid sequence
- The students know and understand the physico-chemical principles that determine protein stability and folding and know the experimental methods to determine these
- The students have a basic knowledge of the principles and formulas relating to enzyme catalysis
- The students have knowledge of and insight in the principles of ligand binding and a number of important methods to study ligand binding
The final grade is composed based on the following categories:
Oral Exam determines 100% of the final mark.
Within the Oral Exam category, the following assignments need to be completed:
Oral examination with written preparation of a general open question, covering multiple parts of the course, and a number of more specific smaller questions.
This offer is part of the following study plans:
Master of Bioengineering Sciences: Cell and Gene Biotechnology: Medical Biotechnology (only offered in Dutch)
Master of Bioengineering Sciences: Cell and Gene Biotechnology: Molecular Biotechnology (only offered in Dutch)
Master of Bioengineering Sciences: Cell and Gene Biotechnology: Agrobiotechnology (only offered in Dutch)
Master of Bioengineering Sciences: Chemistry and Bioprocess Technology: Food Biotechnology (only offered in Dutch)
Master of Bioengineering Sciences: Chemistry and Bioprocess Technology: Chemical Biotechnology (only offered in Dutch)
Master of Bioengineering Sciences: Chemistry and Bioprocess Technology: Biochemical Biotechnology (only offered in Dutch)
Master of Biology: Molecular and Cellular Life sciences (only offered in Dutch)
Master of Biology: Molecular and Cellular Life sciences