Study Guide@lith
 

Linköping Institute of Technology

 
 
Valid for year : 2016
 
TFKE48 Biomolecular Disease Processes, 6 ECTS credits.
/Biomolekylära sjukdomsprocesser/

For:   KeBi   PRO  

 

Prel. scheduled hours: 54
Rec. self-study hours: 106

  Area of Education: Science

Main field of studies: Chemistry, Chemical Biology

  Advancement level (G1, G2, A): A

Aim:
The course aims to provide knowledge of biomolecular processer of common degenerative diseases (Alzheimer´s disease, type II diabetes) and rare diseases (systemic and familial amyloidoses) which collectively are caused by misfolded protein molecules.After the course the student is able to:
  • explpain with deep insight of molecular processes concerning protein misfolding.
  • explain with deep insight how mutations influence protein conformational changes,
  • give avenues for therapeutic strategies against different diseases.


Prerequisites: (valid for students admitted to programmes within which the course is offered)
Protein chemistry. Three years of Chemistry / Chemical biology program or equivalent program

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 contains a number of lectures and a seminar series with active participation of the students. A minor laboratory course is also included.

Course contents:
The course handles the background of a group of human diseases known as the amyloidoses or protein conformational diseases. The links between protein structure, the biophysical and chemical properties of proteins and the link from mutation to conformational change are studied in detail with a number of examples from human diseases.
Proteins studied in detail are: amyloid-beta (Alzheimer�?Ts disease); prion protein (Creutzfeldt Jakob disease); BR12 (familial brittish and danish dementia); immunoglobulin (primary systemic amyloidosis); transthyretin (familial amyloidotic polyneuropathy); high density lipo proteins, amyloid-A (secondary amyloid-A amyloidosis), apoAII; gelsolin (Finnish familial amyloidosis); lysozyme (Inhereted non-neuropathic amyloidois); fibrinogen (inherited nephropathic amyloidosis); beta-2-microglobulin (dialysis related amyloidosis), cystatin-c (heritable cystatin-c amyloid angiopathy), islet amyloid poly peptide (type II diabetes).
The laboratory course contains experimental studies of amyloid fibrils.


Course literature:
Book: �?�Amyloid Proteins. The beta-sheet conformation and disease�?� vol. 2. Editor Jean D. Sipe (Whiley, VCH), and scientific articles.

Examination:
Written examination
Laboratory work
5 ECTS
1 ECTS
 



Course language is Swedish/English.
Department offering the course: IFM.
Director of Studies: Magdalena Svensson
Examiner: Peter Nilsson

Course Syllabus in Swedish

Linköping Institute of Technology

 


Contact: TFK , val@tfk.liu.se
Last updated: 08/23/2016