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Valid for year : 2008
 
TFKE35 Biostructural technologies, 6 ECTS credits.
/Biomolekylär strukturanalys/

For:   BKM   KeBi   PRO  

 

Prel. scheduled hours: 60
Rec. self-study hours: 100

  Area of Education: Science

Subject area: Chemistry
  Advancement level (G1, G2, A): A

Aim:
The objectives of the course is to provide comprehensive knowledge in the following areas:
  • Master and be able to 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.
  • Interprete, judge and evaluate experimental results.
  • Propose and motivate an optimal strategy for solving a given problem within structural biology or bioorganic chemistry.
  • Understand and use literature within biomolecular structural analysis where the methods have been applied.


Prerequisites: (valid for students admitted to programmes within which the course is offered)
Organic chemistry 2 or similar. Biochemistry 1 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.
Organisation:
Lectures, lessons, seminars, demonstrations/practice, and short written tests.

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.

Course literature:
Nuclear Magnetic Resonance. P. J. Hore. Oxford Science Publications 1995. Compendium.

Examination:
Written examination
Written test
 4,5 ECTS
1,5 ECTS
 


Course language is Swedish.
Department offering the course: IFM.
Director of Studies: Stefan Svensson
Examiner: Nils-Ola Persson

Course Syllabus in Swedish

Linköping Institute of Technology
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Contact: TFK , val@tfk.liu.se
Last updated: 05/05/2014