BMB506: Protein chemistry (5 ECTS)

STADS: 01000601

Level
Bachelor course

Teaching period
The course is offered in the autumn semester.
First quarter.

Teacher responsible
Email: jens.andersen@bmb.sdu.dk

Timetable
Group Type Day Time Classroom Weeks Comment
Common I Monday 10-12 U20 36-40
Common I Thursday 12-14 U20 35-41
S1 TE Wednesday 14-16 U43 40
S1 TE Wednesday 14-16 U26 41
S1 TE Friday 08-10 U42 35-38
S1 TE Friday 08-10 U48a 39
S2 TE Tuesday 08-10 U49C 35-39
S2 TE Tuesday 12-14 U49C 40
S2 TE Tuesday 12-14 U28 41
S3 TE Wednesday 16-18 U17 40-41
S3 TE Thursday 08-10 U49D 39
S3 TE Friday 13-15 U14 35-37
S3 TE Friday 13-15 U17 38
S4 TE Monday 14-16 U17 36-41
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Prerequisites:
None

Academic preconditions:
Kemi 1 – Fundamental Chemistry (KE501) and Biology – from molecules to ecosystems has to be passes (BB501). Biomolecular chemistry (BMB501) should be known.

Course introduction
To give an introduction to the structure and function of proteins and how they work in a cellular and physiological context through interactions with proteins and other biomolecules.

Qualifications
• Understand the relationship between protein structure and function
• Understand the basic structural elements of a protein and how they have evolved through evolution, how they fold or misfold, and how their structure in determined experimentally.
• Understand how proteins localize within a cell and how they interact with proteins and other biomolecules such as DNA and RNA and how they form protein complexes.
• Understand how protein works in a larger cellular and physiological context exemplified by the immune system.
• Have knowledge about methods to study proteins experimentally and computationally.
• Know how to use tools to visualization the tertiary structure of proteins.
• Understand how knowledge about the protein-function can be used in the development of drugs directed against proteins.

Expected learning outcome


Subject overview
Protein structure
• Tertiary and Quantinary structure
• Determination of protein structure by NMR and X-ray crystallography
• Protein motifs, folds, domains and subunits
• Examples of protein structure

Protein foldning
• Protein foldning pathways
• Chaperones
• Protein dynamics
• Protein struktural evolution
• Prediction of protein structures
• Conformationelle diseases

Struktur og funktion
• Examples of struktur-funktion relationships
• Protein complexes
• Protein topology og methods for in vivo localization of proteins

Molecular physiology
• The immun system
• Mobility
• Blood koagulation

Post translational modificatons of proteins
• Phosphorylation
• Glycosylation

Protein degradation
• Proteases involved in protein turnover
• Lysosomes
• Ubiquitin-proteasom system

Metods in protein chemistry
• Introduction to proteomics
• Introduction to bioinformatic
• Introduction to protein engineering

Literature
  • Berg, Tymoczko & Stryer : Biochemistry, 6th edition, Freeman, 2006.


Syllabus
See syllabus.

Website
This course uses e-learn (blackboard).

Prerequisites for participating in the exam
None

Assessment and marking:
Assignments, essay and oral examination, external censor and marks following the 7-scale. The Assignments has to be passed to qualify for the exam. The essay is prepared in groups of 2-3 persons which are then examined together but evaluated individually.

Expected working hours
The teaching method is based on three phase model.

Forelæsninger (24 timer), eksaminatorier (12 timer) og obligatoriske regneøvelser indenfor proteiners tertiære struktur ved brug af computer (4 x 2 timer).
Educational activities

Language
No recorded information about the language used in the course.

Course enrollment
See deadline of enrolment.

Tuition fees for single courses
See fees for single courses.