After completion of the course, the student:|
1. knows mathematical concepts used in NMR, in particular;
· use of spin operators, spin Hamiltonian, matrix representation of spin operators
· quantum mechanical description of a J-coupled spin system (weak and strong coupling)
· calculating a NMR spectrum (energy levels, transition probability)
2. knows modern methods to describe NMR experiments, in particular;
· product operator formalism, shape/meaning of product operators, coherence transfer
· time evolution of product operators (effect of pulses, evolution under the spin hamiltionian)
· description of NMR pulse sequences using product operators
· multiple quantum coherence
3. knows basic NMR experiments and building blocks (using product operators), in particular;
· spin-echo experiments (with and without J-coupling)
· homonuclear 2D NMR (COSY, double-quantum filtered COSY, NOESY, TOCSY)
· heteronuclear 2D NMR (HSQC, HMQC)
· basic 3D NMR experiments (NOESY-HSQC, HNCO)
4. is acquainted with advanced topics in modern biomolecular NMR literature, in particular
· methods (pulsed field gradients, TROSY)
· interactions (residual dipolar coupling)
· relaxation theory (modelfree analysis, cross-correlated relaxation)
· paramagnetic NMR (pseudo-contact shifts, paramagnetic relaxation enhancement)
Nuclear magnetic resonance is a very powerful and versatile technique for investigating the structure and dynamics of biomolecules such as proteins and their complexes in solution and even in more solid-like environments, such as membranes. The importance of NMR in biomolecular sciences and in particular in structural biology has been recognized by the attribution of the 2002 Nobel price in chemistry to K. Wüthrich (ETH Zürich).
The course will give a theoretical basis for describing high-resolution NMR experiments, as used in modern NMR spectroscopy. For this we will introduce the use of the product operator formalism. This part of the course will be based on selected chapters (mainly Ch. 3-5) of the following book: NMR: The Toolkit, P.J. Hore, J.A. Jones and S. Wimperis. Oxford Chemistry Primers, a primer (Spin Mechanics, NMR Department) and handouts. The emphasis will be on applications of modern 2D and 3D NMR methods for structural studies of proteins, but the theoretical background is also essential for understanding modern NMR experiments in us in organic and bioorganic chemistry for structural analysis. In the second part of the course we will treat techniques used for studying protein dynamics (NMR relaxation, hydrogen/deuterium exchange) and advanced methods, used in current protein NMR spectroscopy (pulsed-field gradients, residual dipolar couplings, cross-correlated relaxation, Trosy, pseudo-contact shifts).
The course of 2 weeks will be given in workshop style, combining lectures in the morning and assignments in the afternoon. The course can be attended by max. 20 students. The students are expected to actively participate in all sessions and make one assignment at home each day.
Requirements 'Structuuranalyse' (Chemistry/Biology 2nd year) or equivalent level is mandatory and the Structural Biology course (Chemistry/Biology 3rd year) is highly recommended. We assume that the students are familiar with the fundamental concepts of NMR described in those two courses. A useful background is provided in Chapters 1-3 and 6 of P.J. Hore's Oxford Chemistry Primer on NMR.
|Je moet voldoen aan de volgende eisen|
- Toelatingsbeschikking voor de master toegekend
Voorkennis kan worden opgedaan met
|We assume students are familiar with the fundamental concepts of NMR described in those two courses.|
Bronnen van zelfstudie
|Structural Analysis course mandatory, and Structural Biology highly recommended.|
|Chapters 1-3 and 6 of P.J. Hore's Oxford Chemistry Primer on NMR.||Verplicht materiaal-Aanbevolen materiaal|
|NMR: The Toolkit, P.J. Hore, J.A. Jones and S. Wimperis. Oxford Chemistry Primers, a primer (Spin Mechanics, NMR Department)|