| TFKE41 |
Proteomics, 6 ECTS credits.
/Proteomik/
For:
KeBi
MOL
PRO
|
| |
Prel. scheduled
hours: 60
Rec. self-study hours: 100
|
| |
Area of Education: Science
Main field of studies: Chemical biology
|
| |
Advancement level
(G1, G2, A): A
|
|
Aim:
The aim of the course is to provide a broad knowledge of methods and issues within proteomics. Many of the basic methodological principles (genetic, biochemical, analytical chemical and bioinformatic) have been introduced in earlier courses, but here the student learns how these principles are used within a currently very expansive research area: Global characterisation of the proteome with regard to protein abundance, function, regulation, interactions and localisation in different cell types. Transcriptomics is also discussed. To pass the course, the student should be able to
- describe the relevance and distinctive character of proteomics as well as describe and discuss applications of modern methods and strategies to analyse the transcriptome and the proteome
- identify proteins and peptides using mass spectra and genome databases
- use homology modelling to predict a protein structure
- summarise the contents of selected original proteomics literature, interpret its message and review it critically
|
|
Prerequisites: (valid for students admitted to programmes within which the course is offered)
Admission to advanced level studies in Chemical Biology.
Protein chemistry and gene technology. Basic knowledge of analytical chemistry and bioinformatics is also recommended.
Note: Admission requirements for non-programme students usually also include admission requirements for the programme and threshhold requirements for progression within the programme, or corresponding.
|
|
Organisation:
The course consists of lectures, seminars, demonstrations, a laboratory exercise and two home assignments.
|
|
Course contents:
Quantitative mRNA-analysis with DNA microarrays, SAGE and RNAi. Identification and quantitative analysis of cellular protein contents using multi-dimensional separation methods (2DGE, 2DLC), enzymatic cleavage, MS-analysis and genome databases. Protein quantification using isotope labelling and MS. Analysis of post-translational modifications. Characterisation of changes of the cellular protein contents following changes in the environment, for e. g. identification of disease markers. Analysis of protein interactions using affinity chromatography, Y2H analysis and protein microarrays. Structural proteomics with homology modelling.
|
|
Course literature:
Twyman, R. M.; "Principles of Proteomics". Original articles.
|
|
Examination: |
|
Written examination Laboratory work Home assignments Presentation of a scientific article |
3 ECTS 1 ECTS 1 ECTS 1 ECTS
|
| |
|
|
Course language is English.
Department offering the course: IFM.
Director of Studies:
Examiner: Karin Enander
Course Syllabus in Swedish
|