After completion of this course you will be able to
- Describe the most common post-translational protein modifications and their biological functions
- Describe the molecular details of (bio)chemical methods to introduce or modify (artificial) post-translational modifications and how these are used to answer specific biological questions
- Know the analytical methods used in the field of chemical biology and apply them in the correct context to study protein (post-translational) modifications
- Read, understand and present relevant scientific literature aimed to study post-translational modifications with the use of chemical (biology) approaches
- Compose a creative, well-explained and thoroughly-thought research proposal for a relevant biological question related to the post-translational protein modification by methods discussed during the lectures.
Proteins are modified in several ways after ribosomal translation. Post-translational modifications include trimming, splicing, phosphorylation, glycosylation, oxidation, addition of membrane anchors, fusion with other proteins, alkylation, acetylation, and many other types of modification. As a result of such modifications, the potential diversity of the proteome, the complete collection of all proteins in a cell, tissue or organism, greatly exceeds the number of genes in the genome. Proteomes vary considerably between different cell types and tissue samples from the same organism. Chemical biology seeks to understand such differences.
In this course several types of post-translational modifications, methods to study such modifications and technologies to manipulate proteins based upon such modifications will be introduced.