English

If sufficient demand

The aim of the course is for the student to acquire advanced knowledge about Nuclear Magnetic Resonance (NMR) theory and applications in studies of bio-macromolecular structure and dynamics. The course focuses on methods for studying proteins, but the underlying theory is equally applicable to essentially any molecule in the liquid phase.

The course begins with basic theory on NMR, including an introduction to quantum mechanics, quantum statistical mechanics, the density matrix and product operator formalisms. The course then covers the theory of multi-dimensional spectroscopy, including frequency labeling of coherences, coherence transfer and mixing, and coherence pathway selection. The course also covers experimental techniques and practical aspects, including data acquisition and data processing.

understand and be able to explain the basic principles of multi-dimensional NMR spectroscopy
have knowledge about the use of the density matrix and product operator formalisms for interpreting any multi-dimensional NMR pulse sequence.
have knowledge on methods for achieving coherence order and pathway selection.
have knowledge on how to process NMR data to yield multi-dimensional spectra.
have knowledge on multi-dimensional NMR experiments useful for atom-specific resonance assignments and molecular structure determination.

be able to interpret the multi-dimensional NMR pulse sequences in terms of the density matrix and product operator formalism.
be able to design novel NMR pulse sequences for the purpose of acquiring a given type of NMR data.
be able to make informed decisions on suitable combinations of NMR experiments to achieve atom-specific resonance assignments of proteins (or other macromolecules) of a particular type (size, spectral resolution, etc)
be able to process multi-dimensional NMR data
be able to adequately present results and interpretations of NMR experiments both written and verbally.

be able to critically assess the outcome of an NMR experiment in terms of precision and accuracy, plausibility and applicability.
be able to critically review research literature that describes application of NMR.
have the ability to choose the NMR technique that is most appropriate to apply to a given research problem.
have a broad insight into applications outside his or hers own principal research area.
be able to actively take part in qualified discussions about applications and interpretations of NMR experiments.

Seminars

Project

Self-study literature review

The course is organized around seminars or discussion meetings where groups of students present the assigned reading material.
The course also includes a project, where each student will analyze an NMR pulse sequence from the research literature.

Written report

Written assignments

Students will solve home assignments during the course.

At the end of the course, each student will be assigned a recent research publication, which should be analyzed in detail using the theory learnt in the course and described in a written report.

Failed, pass

KFKN01, Magnetic Resonance — Spectroscopy and Imaging, or an equivalent course.

Mathematics corresponding to curriculum in the K or B programs at LTH.

J, C., WJ, F., AG, P., M, R. & NJ, S.: Protein NMR Spectroscopy. Principles and Practice, 2nd Edition. Elsevier Academic Press, 2007. ISBN 9780121644918.

The textbook will be complemented with review articles distributed during the course.

The course will be offered provided that a sufficient number of students have shown an interest. Normally, this would entail at least 3-4 students in order for the peer instruction element to work well.

KFK001F

 -03-19

Margareta Sandahl