NKED76 Protein Structure and Function 2007

Study Guide@lith

Valid for year : 2007

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 (G1, G2, A): A
	Aim: The objectives of the course is to provide comprehensive knowledge in the following areas: Protein chemistry, protein engineering, structure and function relationships as well as methodologies for characterization of proteins. After studies well learned the student will have proficiency to: Identify structure motifs and from this draw conclusions regarding the structure and function of proteins. Search for information from various data bases to visualize protein structures for studies of topologies and structure-function relationships. Comprehend the fundamental mechanisms of protein folding and to have a basic understanding of the factors determining the stability of a protein. Use modern laboratory techniques for studies and interpretation of the conformation of proteins.
	Prerequisites: (valid for students admitted to programmes within which the course is offered) Approved Biochemistry 1 or equivalent. Attended Biochemistry 2 och Biochemistry 3 or equivalent. 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. Proteinfoldning is investigated as a project.
	Course literature: C. Branden and J. Tooze: Introduction to Protein Structure. Laboratory manual
	Examination:
	Written examination Laboratory course	2,5 p 2,5 p	/ /	4 ECTS 3,5 ECTS

	The exercises of the written examination and the test elucidate how well the student perform the the demands of the course.
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
Contact: TFK , val@tfk.liu.se Last updated: 05/30/2007