| TFKE35 |
Biostructural technologies, 6 ECTS credits.
/Biomolekylär strukturanalys/
For:
KeBi
PRO
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Prel. scheduled
hours: 36
Rec. self-study hours: 124
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Area of Education: Science
Main field of studies: Chemical biology
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Advancement level
(G1, G2, A): A
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Aim:
The course aims at providing the basic theoretical framework for NMR spectroscopy and x-ray crystallography, which is the foundation for structural analysis of proteins and other biomolecules in organic chemistry and structural biology. After completed course, the student should be able to:
- Master and explain important concepts, methods and theories in the determination of molecular structure and dynamics.
- Illustrate and shed light on theoretical concepts with examples from biomolecular analysis.
- Interpret, assess and evaluate experimental results.
- Propose and motivate an optimal strategy for solving a given problem within structural biology or bioorganic chemistry.
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Prerequisites: (valid for students admitted to programmes within which the course is offered)
Organic chemistry continued course. Biochemistry. Protein Chemistry.
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, seminars, demonstrations.
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Course contents:
The NMR part of this course comprises: The NMR phenomenon, resonance, chemical shift, spin-spin couplings (weak and strong), dipolar couplings, nuclear spin relaxation, especially the nuclear Overhauser effect. Dynamic NMR, chemical exchange. Two dimensional NMR spectroscopy, COSY, TOCSY, NOESY. Heteronuclear experiments, HSQC. Analysis of onedimensional and multidimensional spectra. Procedures for structural and dynamical characterization of proteins.
The crystallography part of this course comprises: protein crystallization, including concepts such as unit cell, asymmetrical unit, space group, Miller index, Braggâ?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:
NMR Spectroscopy â?" Principles and Applications to Proteins. P. Lundström, 2012.
Crystallography made Crystal Clear. Gale Rodes. Academic Press 2000, 2nd edition.
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Examination: |
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Written examination
Written test
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4,5 ECTS
1,5 ECTS
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Course language is Swedish/English.
Department offering the course: IFM.
Director of Studies: Magdalena Svensson
Examiner: Patrik Lundström
Course Syllabus in Swedish
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