TFKE48 · 6 credits · Advanced level (A1F) · Kemisk biologi, Kemi
Biomolecular Disease Processes
Active · next start HT 2026
91%
passed the latest ordinary exam
TEN1 · 16 Jan 2026 · 11 students
97%
passed the ordinary exams, all sittings over the last 5 years
TEN1 · 66 students
17%
Harder than 17% of courses at advanced level
Compared with 285 courses at the same level, ordinary exams over the last three academic years. 30 students.
Part of 2 programmes
Exam
TEN1 Written examination
- 5
- 4
- 3
- U
Ordinary exams
97% passed · 66 students
- 91%11
- 100%19
- 92%12
- 100%9
- 100%15
Re-exams
No sittings with at least 5 students.
- Get 4 or 5: 61% (66 students)
Show small sittings (3)
Sittings with fewer than 5 students, often credit transfers or special sittings. They are not part of any figure on this page.
- 0%1
- 0%1
- 100%2
Other modules
Partial exams, hand-ins and labs. They are not part of the figures at the top.
Hand-in or lab
LAB1 Laboratory work
- G
- U
Main rounds
99% passed · 75 students
- 93%14
- 100%19
- 100%14
- 100%9
- 100%19
Later rounds
No sittings with at least 5 students.
About the course
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.
Content
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 and tau (Alzheimer’s disease); prion protein (Creutzfeldt Jakob disease); BRI-2 (familial brittish and danish dementia); immunoglobulin (primary systemic amyloidosis); transthyretin (familial amyloidotic polyneuropathy); high density lipo proteins, amyloid-A (secondary amyloid-A amyloidosis), apoAII; lysozyme (Inhereted non-neuropathic amyloidois); fibrinogen (inherited nephropathic amyloidosis); beta-2-microglobulin (dialysis related amyloidosis); alpha-syniuclein (Parkionsos disease); islet amyloid poly peptide (type II diabetes). The laboratory course contains experimental studies of amyloid fibril model systems.
- Examiner
- Sofie Nyström
- Scheduled hours
- 54 h
- Main field of study
- Kemisk biologi, Kemi