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Aim

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.

Goals

Knowledge and Understanding

For a passing grade the doctoral student must:

  • 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.

    Competences and Skills

    For a passing grade the doctoral student must:

  • 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.

    Judgement and Approach

    For a passing grade the doctoral student must:

  • 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 her own principal research area.

  • be able to actively take part in qualified discussions about applications and

    interpretations of NMR experiments.

Course Syllabus 2024

Course Contents

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.

Course Literature

Cavanagh J, Fairbrother WJ, Palmer AG, Rance M, Skelton NJ. Protein NMR Spectroscopy. Principles and Practice, 2nd Edition. Elsevier Academic Press, 2007. ISBN 9780121644918.

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

Instruction Details

Types of instruction

Self-study followed by discussion in class, home assignments, self-study literature review project. 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.

Weekly class sessions will be conducted on Zoom. We may decide on 1–2 in person meetings at Lund University.

Examination Details

Examination formats

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.

Grading scale: Pass, Fail Examiner: Mikael Akke

Course instructors

Professor Mikael Akke, Doc. Göran Carlström.

Admission Details

Admission requirements: KFKN01, Magnetic Resonance — Spectroscopy and Imaging, or an equivalent course.
Assumed prior knowledge: Mathematics corresponding to the curriculum in the K or B programs at LTH.

Registration

Please register by e-mail: mikael.akke@bpc.lu.se
PhD students enrolled at Lund University should register via Ladok.

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Course Syllabus 2024

Course Outline

  1. W16  Cavanagh Ch. 1

  2. W17  Cavanagh Ch. 2.1–5,

    Akke & Halle “Quantum Picture of NMR: Dynamics of Coupled Spins”

  3. W18  Cavanagh Ch. 2.6–2.8

  4. W19  Cavanagh Ch. 3

  5. W20  Cavanagh Ch. 4

  6. W21  Cavanagh Ch. 7.1–7.3

  7. W22  Cavanagh Ch. 7.4–7.6

    Review articles on triple-resonance 3D/4D experiments

  8. W23  Cavanagh Ch. 9

  9. W24  Self-study: review of assigned paper

  10. W25  Self-study, continued. Written report

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