Introductory description

Nuclear magnetic resonance (NMR) in both solution and the solid state as well as electron paramagnetic resonance (EPR) will be described. The course will cover the underlying theory of the experiments as well as practical aspects of recording spectra and their interpretation. The importance of magnetic resonance across science, in, e.g., organic chemistry, pharmaceuticals and proteins, will be demonstrated.

Module aims

Outline syllabus

This is an indicative module outline only to give an indication of the sort of topics that may be covered. Actual sessions held may differ.

(1) Foundations of Nuclear Magnetic Resonance (NMR) (recap of material presented in CH921), e.g., spin angular momentum, Larmor frequency, instrumentation requirements, NMR interactions: chemical shifts, J and dipolar couplings, quadrupolar, Fourier transformation).

(2) Introduction to two-dimensional NMR (how the experiment works, phase- and amplitude modulation, schematic appearance of, e.g., NOESY spectra).

(3) Interpretation of solution-state NMR spectra of moderately sized organic molecules (e.g., diamagnetic and paramagnetic shieldings on 1H and 13C chemical shifts, effects of multiple bonds and rings, the -gauche effect, DEPT for interpreting 13C spectra, J coupling: 1J, 2J, 3J and 4JHH. 1JCH, Karplus relation, decoupling, both homo- and heteronuclear, 2D COSY for complex cases).

(4) Chemical exchange (effect on NMR spectra, extraction of dynamic information).

(5) NMR relaxation and saturation (experiments for measuring T1 and T2; solvent suppression).

(6) Basic overview of methods for calculating NMR chemical shifts.

(7) Using NMR for protein structure determination (2D experiments, the nuclear Overhauser effect).

(8) Basic concepts in solid-state NMR (magic-angle spinning, cross polarisation, 2D methods, applications to pharmaceuticals and biosolids).

(9) Introduction to electron paramagnetic resonance (basic concepts and hardware, dynamic nuclear polarisation).

Learning outcomes

By the end of the module, students should be able to:

• Understand the physical basis of magnetic resonance experiments and the role of the different elements of spectrometer hardware
• Assign NMR spectra, so as to identify the structure of small to moderately sized organic molecules
• Appreciate the wide applicability of magnetic resonances techniques

Indicative reading list

M. H. Levitt, "Spin Dynamics", 2nd edition, Wiley, Chichester 2008.

P. J. Hore, "Nuclear Magnetic Resonance", Oxford University Press, Oxford 1995.

J. Keeler, "Understanding NMR Spectroscopy", Wiley, Chichester 2005.

T. D. W. Claridge, "High-Resolution NMR Techniques in Organic Chemistry", Pergamon, Oxford 1999.

J. Cavanagh, W.J. Fairbrother, A.G. Palmer III, M. Rance, N. J. Skelton, "Protein NMR Spectroscopy Principles and Practice", 2nd edition, Elsevier, London 2007.

M. J. Duer, "Introduction to Solid-State NMR Spectroscopy", Blackwell, Oxford 2004.

P.H. Rieger, "Electron Spin Resonance Analysis and Interpretation", RSC, Cambridge 2007.

Subject specific skills

Understand the physical basis of magnetic resonance experiments and the role of the different elements of spectrometer hardware
Assign NMR spectra, so as to identify the structure of small to moderately sized organic molecules
Use relevant databases and prediction programs
Appreciate the wide applicability of magnetic resonances techniques

Transferable skills

TBC