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Linköping Institute of Technology

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Valid for year : 2004
 
NKED76 Protein Structure and Function, 7,5 ECTS credits.
/Proteiners struktur och funktion/

For:   Bio   BKM   Kem  

 

Prel. scheduled hours: 60
Rec. self-study hours: 140

  Area of Education: Science/Technology

Subject area: Chemistry

  Advancement level (A-D): D

Aim:
The course will give comprehensive knowledge in protein chemistry and protein engineering. The relationship between the protein structure and biological function is studied in particular as well as their physicochemical properties and how these characteristics can be employed to explore the properties of proteins.

Prerequisites: (valid for students admitted to programmes within which the course is offered)
Attended NKEC52 Biochemistry 2

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 is divided into a theoretical and a laboratory part in order to give opportunity to deeper and more intergrated studies. The theoretical education is given as lectures and seminars with active participation from the students. Training in computer simulation and molecular modeling is also given as well as exercises with 3-dimensional structures of proteins. The students will during the laboratory course come into contact with modern analysis methods and instruments used in characterization of proteins. Conventional laboratory protocols are used as instructions for the analyses, but also scientific articles to give training in independent experiment planning. A literature seminar is held during the course

Course contents:
The following areas are treated during the lectures: Structure motifs of proteins like alpha domain structures, alpha/beta structures, antiparallel betastructures, DNA-recognizing proteins, multifunctional enzymes, nucleotide binding enzymes, membrane proteins, receptor proteins, antibodies, viru structures. Furthermore, evolution of proteins, prediction of protein structure, design of new proteins, protein folding, structure-function studies of engineered proteins and enzyme catalysis is treated. Proteins are characterized during the laboratory course with modern methodology as e.g. SDS-polyacrylamide gelelectrophoresis, Western blotting, fluorescence measurements, and circular dichroism (CD) spectroscopy.

Course literature:
C. Branden and J. Tooze: Introduction to Protein Structure. Laboratory manual

Examination:
Written examination
Laboratory course
2,5 p
2,5 p
 



Course language is Swedish.
Department offering the course: IFM.
Director of Studies: Stefan Svensson
Examiner: Uno Carlsson

Course Syllabus in Swedish

Linköping Institute of Technology

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Contact: TFK , val@tfk.liu.se
Last updated: 07/22/2004