8BKA61 · 6 credits · Advanced level (A1X) · Medicinsk biologi
Protein Structure and Function
Active · next start VT 2027
95%
passed the latest regular sitting
61WE · 23 Mar 2026 · 38 students
89%
passed the regular sittings, all sittings over the last 5 years
61WE · 124 students
32%
Harder than 32% of courses at advanced level
Compared with 285 courses at the same level, ordinary exams over the last three academic years. 75 students.
Part of 1 programme
Other module
61WE Written examination
- 5
- 4
- 3
- U
Main rounds
89% passed · 124 students
- 95%38
- 89%37
- 84%32
- 82%17
Later rounds
56% passed · 32 students
- 43%7
- 77%13
- 60%5
- 29%7
- Pass a later round: 56% (32 students), compared with 89% (124 students) on the ordinary exam
- Get 4 or 5: 62% (156 students)
Show small sittings (11)
Sittings with fewer than 5 students, often credit transfers or special sittings. They are not part of any figure on this page.
- 100%1
- 0%3
- 75%4
- 100%2
- 100%1
- 100%1
- 75%4
- 100%1
- 25%4
- 100%1
- 75%4
About the course
Aim
Knowledge and understanding
Having completed the course, the student is expected to be able to:
- Identify common protein structural motifs in relation to structure and function
- Explain protein folding mechanisms and the factors that determines protein stability
Skills and abilities
On completion of the course, the student shall be able to:
- From laboratory data calculate protein stability and ligand interactions
- Obtain information from databases to be able to visualize protein structures and compare protein sequences
Judgement ability and approach
On completion of the course, the student shall be able to:
- Critically review detailed chemical and physical properties of proteins to draw conclusions about dynamic, structure and function
Content
The course gives advanced knowledge in protein chemistry, protein engineering, structure- functional relationships, protein biophysical-chemical characteristics and techniques to characterize proteins. This includes studies of different protein structural motifs (like alpha- domain structures, alpha/beta structures and anti-parallel protein structures) that comprises membrane proteins and prediction of protein structures. Further, the course deals with physical- chemical properties of proteins and methods to study these properties. Elements of the course are chemical properties of polypeptides, protein engineering, physical interactions that determines protein properties, the role of hydrophobic interactions, flexibility in protein structures, protein stability, protein folding mechanisms, interaction with other molecules and enzyme catalysis. At computer laboratory sessions searches in databases are made to study three-dimensional protein structures and to simulate different structures.
The course encompasses the fields of biochemistry and protein chemistry.
- Examiner
- Lars-Göran Mårtensson
- Main field of study
- Medicinsk biologi