Deze cursusinformatie geeft aan hoe het onderwijs zal verlopen bij pandemieniveau code geel en groen.
Als er tijdens het academiejaar aangepast wordt naar code oranje of rood, zijn er wijzigingen mogelijk o.a. in de gebruikte werk - en evaluatievormen.

Protein technology and proteome analysis

Course Code :2002FBDBIC
Study domain:Biotechnology
Academic year:2020-2021
Semester:1st semester
Contact hours:60
Study load (hours):168
Contract restrictions: Exam contract not possible
Language of instruction:English
Exam period:exam in the 1st semester
Lecturer(s)Sylvia Dewilde
Eva Geuens
Xaveer Van Ostade
Stuart Maudsley

3. Course contents *

The theoretical aspects will be demonstrated using practica. In the first part of the course, the focus will be on the study of proteins:

-     methods for protein extraction

-     chemical modification of proteins: e.g. (i) chemical modification of the amino acids cysteine or lysine by vinylpiridinylation and modification by maleinic acid respectively, (ii) biotinylation of proteins

-     purification of protein mixtures with limited complexity using ion-exchange and reversed phase chromatography. The purity can be checked using SDS-PAGE

-         making a strategy for cleaving proteins

-         separation of limited complex peptide mixtures using reversed phase chromatography

-        N-terminal sequencing of proteins and peptides by Edman degradation

-         Examples of affinity-chromatography

-         technologies to determine protein-protein interaction networks


In the following part of the course, proteomics will be discussed. Focus will be on:

-           separation techniques of complex protein mixtures using gelelectrophoreses or chromatography

-           identification techniques based on mass-spectrometry

-           discussion of different strategies for comparing protein-profiles (ICAT, iTRAQ, DIGE, O16/O18 labelling)

-           Ion mobility mass spectrometry to study protein flexibility and lipids

-           proteomic methods to determine posttranslational modifications in proteins

These theoretical lectures will be followed by practical exercises: i) labwork (sample handling and gel electrophoreses), ii) demonstrative practical work (2D-microcapilliary chromatography and mass-spectrometry).