| TFKE24 | Biostructural technologies, 7,5 ECTS credits. /Biomolekylär strukturanalys/ |
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Prel. scheduled
hours: 60 |
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Area of Education: Science Subject area: Chemistry |
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| Advancement level
(A-D): C
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| Aim: After this course, the student should possess basic knowledge in high-resolution NMR spectroscopy as well as x-ray crystallography, both in theory and practice. The course forms a basis for applied structural analysis of proteins and biomolecules within organic chemistry, biochemistry and structural biology. After the course, the student will master important concepts, methods and theories for the determination of molecular structure and dynamics, evaluate and judge experimental results, acquire and evaluate advanced literature within biomolecular structural analysis, and choose an optimal strategy for solving a given problem in structural biology or bioorganic chemistry. |
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| Prerequisites: (valid for students admitted to programmes within which the course is offered) Organic chemistry 2 (NKEB22) or similar. Biochemistry 1 (NKEA28) or similar. 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: Lectures, lessons, seminars, demonstrations/practice, and short written tests. |
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| Course contents: The NMR part of this course comprises: the NMR phenomenon, resonance, chemical shift, spin-spin coupling (strong and weak), dipolar coupling, chemical exchange, spin relaxation, in particular the nuclear Overhauser effect, quadrupolar relaxation. NMR dynamics, Two-dimensional NMR spectroscopy, correlation experiments, COSY, NOESY, TOCSY, HSQC. Heteronuclear experiments. Procedures in structural analysis of small bioorganic molecules and proteins. Instrumental demonstration and practice. The crystallography part of this course comprises: protein crystallization, including concepts such as unit cell, assymetrical unit, space group, Miller index, Bragg�?Ts law and Evald sphere. Furthermore, the entire process of solving a protein structure starting from a protein crystal will be treated, including concepts such as resolution, electron density maps, R-factor, B-factor, heavy metal derivatization and molecular replacement. |
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| Course literature: Nuclear Magnetic Resonance. P. J. Hore. Oxford Science Publications 1995. Compendium. |
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| Examination: | |||
| Written examination (U,3,4,5) Laboratory work (U,G) |
4 p 1 p |
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Course language is Mainly Swedish. 1-2 lectures in English by visiting professors. . Department offering the course: IFM. Director of Studies: Stefan Svensson Examiner: Maria Sunnerhagen Course Syllabus in Swedish |
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