Aims:

This is an advanced module to familiarise the student with modern spectroscopic and mass spectrometric techniques and their applications in materials characterisation. Emphasis is given to those techniques, which are currently most important to chemical research both in industry and academia. The students should be able to understand the basic physical principles of these techniques and to decide which combination of techniques is best employed to tackle a particular problem of materials/chemicals characterisation.  

The aims of the module are:

-         To explain main principles of Nuclear Magnetic Resonance Spectroscopy from the point of view of interactions of nuclear spins in solution and in the solid state.

-         To introduce a variety of modern NMR methods for the determination of chemical structu re and intermolecular interactions in complex organic molecules, polymers and solids.

-         To introduce the concept of magnetic resonance imaging and its industrial and biomedical applications.

-         To explain main principles of Mass spectrometry, modern instrumentation and ionisation techniques.

-         To enable students to decide which techniques of mass spectrometry should be applied to a particular problem.

-         To enable students to interpret mass spectra of a range of different compound classes.

-         To present an overview, and in some selected cases, detailed knowledge on modern surface spectroscopic techniques.

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

-         Discuss the behaviour of nuclear spins and their ensembles in external magnetic field;

-         Discuss main magnetic interactions influencing the appearance of NMR spectra;

-         Describe the structure of modern NMR spectrometers;

-         Explain the concepts of data acquisition and processing;

-         Show an understanding of chemical shift, magnetisation, rotating frame of reference, scalar coupling, basic pulse programming;

-         Explain the principles of determination of T₁ and T₂ relaxation times and calculate T₁ and T₂ from the NMR dat a;

-         Describe main one-dimensional experiments and interpret the spectra;

-         Explain the nuclear Overhauser effect and its use in analysis of complex organic molecules;

-         Explain main principles of two-dimensional experiments and interpret the 2D spectra recorded for both liquids and solids;

-         Explain the concept of coherence and coherence transfer;

-         Discuss the differences in acquisition of solution and solid-state NMR spectra;

-         Explain the MAS, cross-polarisation and decoupling methods used for solids;

-         Describe experiments suitable for the analysis of int ernuclear connectivites, distances and mobility in organic and inorganic solids;

-         Understand the concept of magnetic resonance imaging and its industrial and biomedical applications.

-         Describe the function of modern mass spectrometers.

-         Explain all major ionisation techniques used in mass spectrometry.

-         Decide which ionisation technique should be applied to a particular problem.

-         Expalin reactions occurring in mass spectrometers (rearrangements and fragmentations).

-         Interpret mass spectra.

-         Explain the role of mass spectrometry in proteomics research.

-         Explain the use of mass spectrometry in surface characterisation.

-         Explain surface vibrational spectroscopy (IR, RAMAN, SERS)

-         Explain the surface selection rule.

-         Understand XPS and interpret XPS spectra

-         Understand the basics of X-ray fluorescence and Auger Electron Spectroscopy.

-         Understand EDX and EELS and interpret spectra.

-         Critically compare different methods of surface spectroscopy.

-        Solve real research problems in chemistry by the application of Mass Spectrometry and surface spectros copic methods and correctly interpret the results.

NMR (16 lectures, Yaroslav Khimyak)

0. Basics of NMR (1-6)

-         Spins in a magnetic field

-         Vector model of NMR

-         Quantum mechanical description

-         Experimental NMR: nuts and bolts

-         Fourier Transformation and data processing

-         Chemical Shift, Scalar coupling, Dipolar coupling

-         Relaxation (T₁ and T₂ measurements)

1. High Resolution NMR Spectroscopy (7-11)

-&# 160;        Making the spins dance (decoupling, composite pulses)

-         NMR spectra of exchanging and reacting systems

-         Multiple resonance and one-dimensional pulse sequences

-         The nuclear Overhauser effect

-         Two-dimensional NMR and 2D experiments using coherence transfer (application for biomolecules and polymers)

2. Solid-State NMR (12-14)

-         Magnetic interactions in solids (dipolar coupling, chemical shift anisotropy, quadrupolar coupling)

-         Main experimental techniques (magic-angle spinning, heteronuclear dec oupling, homonuclear decoupling, cross-polarisation)

-         Studies of quadrupolar nuclei (high-resolution experiments for half-integer quadrupolar nuclei)

-         Analysis of molecular motions in solids

3. Magnetic resonance imaging (15-16)

-         Producing an image

-         Diffusion and flow

-         Chemical shift imaging

-         Biological use of imaging

-         Biomedical NMR

Mass Spectrometry and Surface Spectroscopies (16 lectures, Heike Arnolds)

1. Mass Spectrometry (7 lectures)

-         Instrumentation and Ionisation Methods (2 lectures)

-         ICP-MS (1 lecture)

-         Mass spectra of small to medium size molecules (2 lecture)

-         Mass spectra of macromolecules (1 lecture)

-         MS in proteomics research (1 lectures)

-         SIMS (1 lecture)

2. Surface Spectroscopies (9 lectures)

-         vibrational surface spectroscopies (IR, Raman, SERS) (3 lect ures)

-         X-ray based surface spectroscopies (XPS, XRF, AugerES) (3 lectures)

-         Electron based surface spectroscopy (EDX, EELS) (3 lectures)

This is a M level course due to its difficulty particularly as a distance learning course. This module differs from the lecture course (CHEM374) in that  students work through the course text book in conjunction with notes mounted on the VITAL website according to the schedule provided. An important M-level addition is that they will be given extra sets of 'M-level' problems both in mass spectrometry and in surface spectroscopy that are related to real research situations in chemistry. The complexity of the NMR problems is very high in CHEM374 so that no additional tasks are needed here. The necessity to solve these problems by distance learning adds significant extra difficulty to the course.

Distance assignments are completed at regular intervals throughout the semester, with marked work and model answers being returned to the students. Problems are dealt with mainly by email; the student's academic and industrial supervisors are also available to help. This distance learning assignment contribute 50 % to the module mark and asessment will be at the "M" level.

1. M. H. Levitt, Spin dynamics.  Basics of nuclear magnetic resonance, John Wiley & Sons, 2002.
2. M. J. Duer,  Solid-state NMR spectroscopy, Blackwell, 2004.
3. R. K. Harris, Nuclear magnetic resonance spectroscopy.  A physicochemical view, Longman, 1997.
4. J. W. Akitt and B. E. Mann, NMR and chemistry.  An introduction to modern spectroscopy, Stanley Thornes, 2000.
5. Book on modern methods of mass spectrometry (to be decided)
6. Attard and Barnes, Surfaces, Oxford Chemistry Primer, Oxford University Press 1998
7. Banwell, McCash, Fundamentals of Molecular Spectroscopy, McGraw-Hill, 1994
8. D. P. Woodruff and T. A. Delchar, Modern Techniques of Surface Science, Oxford University Press, 2001.