NKED27 · 15 credits · Advanced level (A1N) · Kemisk biologi
Protein Chemistry
Active · next start VT 2027
83%
passed the latest ordinary exam
DIT1 · 23 Mar 2026 · 18 students
84%
passed the ordinary exams, all sittings over the last 5 years
DIT1 · 58 students
68%
Harder than 68% 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 3 programmes
Exam
DIT1 Digital examination
- 5
- 4
- 3
- U
Ordinary exams
84% passed · 58 students
- 83%18
- 75%12
- 94%18
- 80%10
Re-exams
No sittings with at least 5 students.
- Get 4 or 5: 67% (58 students)
Show small sittings (8)
Sittings with fewer than 5 students, often credit transfers or special sittings. They are not part of any figure on this page.
- 0%1
- 67%3
- 0%2
- 100%1
- 0%1
- 100%2
- 100%1
- 0%1
Other modules
Partial exams, hand-ins and labs. They are not part of the figures at the top.
Hand-in or lab
LAB1 Protein purification
- G
Main rounds
100% passed · 58 students
- 100%17
- 100%10
- 100%9
- 100%12
- 100%10
Later rounds
No sittings with at least 5 students.
Show small sittings (1)
Sittings with fewer than 5 students, often credit transfers or special sittings. They are not part of any figure on this page.
- 100%4
Hand-in or lab
PRA1 Project work
- G
Main rounds
100% passed · 28 students
- 100%5
- 100%5
- 100%8
- 100%10
Later rounds
100% passed · 25 students
- 100%10
- 100%6
- 100%9
- Pass a later round: 100% (25 students), compared with 100% (28 students) on the ordinary exam
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.
- 100%2
- 100%4
- 100%4
About the course
Aim
The course aims to provide in-depth knowledge in the following areas: The theoretical part deals with protein engineering, structural-functional relationships, the biophysical chemical properties of proteins and methodology for characterization of proteins. The experimental part deals with the expression of cloned proteins and methodology for purification of proteins as well as characterization of these proteins.
After the course, the student is expected to be able to
Theoretical part:
- Identify how proteins are structured
- Use information from different databases to compare amino acid sequences and based on that make predictions related to the biophysical properties of the protein
- Use biophysical measurement data for characterization of proteins
Experimental part:
- Produce and purify cloned proteins
- Formulate problems in the area, which can be answered with experimental methodology
- Work in groups in project form in the laboratory
- Have a reflective, scientific approach to theories and experimental data
Content
In the theoretical part, different structural motifs of proteins are treated, such as alpha domain structures, alpha/beta structures, antiparallel beta structures, multifunctional enzymes, membrane proteins, prediction of protein structures. Furthermore, the course deals with biophysical properties of proteins and methodology for studies of these: chemical properties of polypeptides, protein engineering, physical interactions that determine properties of proteins, i.e., the role of the hydrophobic interaction, the protein structure flexibility, protein stability, protein folding mechanisms, interaction with other molecules, enzyme catalysis.
The experimental part contains protein expression, protein purification, biophysical properties of proteins and methodology for studies of these. Biophysical measurement methods such as fluorescence spectroscopy, circular dichroism (CD) and calorimetry (ITC) are used. Furthermore, sequence analysis and structural modeling are used for analysis of results.
- Examiner
- Lars-Göran Mårtensson
- Scheduled hours
- 89 h
- Main field of study
- Kemisk biologi