| NKED74 | Protein Chemistry, 15 ECTS credits. /Proteinkemi/ |
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Prel. scheduled
hours: 46 |
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Area of Education: Science Subject area: Chemistry |
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| Advancement level
(G1, G2, A): A
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| Aim: The objectives of the course is to provide comprehensive knowledge in the following areas: Protein chemistry, protein engineering, structure and function relationships, physicochemical properties of proteins and methodologies for characterization of proteins. After studies well learned the student will have proficiency to:
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| Prerequisites: (valid for students admitted to programmes within which the course is offered) Approved General Chemistry 1, General Chemistry 2, Organic Chemistry 1, Biochemistry 1. Attended Biochemistry 2 and Biochemistry 3 or equivalent courses. 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. |
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| Organisation: The course is divided into a theoretical and a laboratory part in order to give opportunity to deeper and more intergrated studies.The theory is presented and treated at lectures and seminars with active participation of the students. Three-dimensional structures of proteins and computer simulations are performed in smaller groups. During the experimental part the students work with genetically mutated human proteins cloned in bacteria. The origin of the mutated protein can be proteins that have been mutated by the students in an earlier course in gene technology (NKEC61) or can be provided by the research group. The protein variants are purified and characterised by using modern separation and analysis methodology. The experimental work is guided by laboratory manuals and original scientific articles in order to train independent planning and performance of the experiments. The results of the experimental work is presented and discussed in reports and in a seminar. |
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| Course contents: Theoretical part: Different structure motifs of proteins. DNA-recognising proteins, multifunctional enzymes, nucleotide binding enzymes, virus structures, recognition of antigens by antibodies, membrane proteins, receptor proteins, prediction, engineering and design of protein structures.Studies of physico-chemical properties of proteins and methodology for studies of these properties: Chemical characteristics of polypeptides, protein engineering, posttranslational modification, evolution and origin of proteins, physical interactions determining the properties of proteins, role of hydrophobic interaction, structure determination by X-ray, NMR and CD, conformation flexibility, protein stability, mechanisms of protein folding, interaction with other proteins, enzyme catalysis. Experimental part: Expression of cloned proteins in bacteria, affinity chromatography, SDS gel electrophoresis, fluorescence measurements, circular dichroism (CD) measurements, computer simulation. Site-directed mutated proteins are purified and characterised and the stability is determined. |
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| Course literature: Branden, C. and Tooze, J.: Introduction to protein structure, 2nd edition. Creighton, T.E.: Proteins. Structure and molecular properties. Laboratory manual. |
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| Examination: | ||||
| Written examination, part I Written examination, part II Laboratory course |
2,5 p 2,5 p 5 p |
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4 ECTS 4 ECTS 7 ECTS |
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| 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 |
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