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Course contents

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.
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, Bragg’s 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.

Responsible for this page: Patrik Lundström (patlu@ifm.liu.se)
Last updated: 03/24/13