English

If sufficient demand

The aim of the course is for the student to acquire advanced knowledge about NMR relaxation 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 relaxation, including the random-phase model for transverse relaxation, Bloch-Wangsness-Redfield theory, stochastic processes, correlation functions and spectral density functions, relaxation mechanisms, interference effects, and chemical exchange effects. The course then covers the experimental approaches to study molecular dynamics using NMR relaxation.

understand and explain the basic principles of NMR relaxation
have knowledge about the use of the BWR theory for investigating relaxation processes active for a given density matrix element.
have knowledge about different relaxation mechanisms.
have knowledge about correlation functions and spectral density functions.
have knowledge about multi-dimensional NMR experiments useful for studying molecular dynamics on different time scales.

be able to determine the dominant relaxation mechanisms active in a given NMR relaxation experiment.
be able to design novel NMR pulse sequences for the purpose of acquiring a given type of NMR relaxation data.
be able to make informed decisions on suitable combinations of NMR relaxation experiments to measure dynamic properties on a protein of a particular type (size, spectral resolution, etc)
be able to interpret NMR relaxation data in terms of molecular dynamics (rotational diffusion, order parameters, etc)
be able to adequately present results and interpretations of NMR relaxation experiments both written and verbally.

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

Required: KFKN01, Magnetic Resonance — Spectroscopy and Imaging, or another course at the corresponding level Recommended: Advanced NMR spectroscopy.

Mathematics corresponding to the K or B programs at LTH

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

The course text book will be complemented by review articles.

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

KFK005F

2020-03-19

Margareta Sandahl