The course will illustrate the wide applications of nuclear magnetic resonance (NMR) spectroscopy in the study of structure, dynamics, folding and function of biological macromolecules with a special emphasis on protein analysis.
Course Prerequisites
General and Organic Chemistry at undergraduate level. Special pre-course reading will be provided.
Teaching Methods
Lectures and a set of practical demonstrations at the instrument (Centro Grandi Strumenti) and in the new teaching laboratories of the Department of Molecular Medicine.
Assessment Methods
Written examination paper.
Texts
Thomas C. Pochapsky NMR for Physical and Biological Scientists. Routledge, 394 (2019)
A. Joshua Wand (ed) Biological NMR Part A. Academic Press, 412 pages (2019)
Contents
(i) Introduction (Magnetic properties of nuclei and electrons - precession, RF pulses and spin relaxation - Bloch equations).
(ii) Instrumentation (Instrumental considerations - probes, Fourier transform methods and data processing, Classical and Quantum Descriptions)
(iii) NMR Observables (Scalar Couplings, Chemical Shifts, Introduction to a QM description of NMR, Applications to second order spectra)
(iv) Density Matrices (Product Operator Formalism, Evolution and interpretation, in product operator form, Heteronuclear Correlation, COSY, TOCSY)
(v) Basic Pulse Sequences (Pulse field gradients and extensions to 3D, Triple resonance experiments for proteins, Sequential assignment strategies in proteins)
(vi) Applications (Metabolomics, Chemical Exchange and Diffusion, Protein Folding and Amide Exchange, Drug Discovery, Imaging (MRI), Spin Relaxation and NOE, Spin Relaxation in Proteins, Residual Dipolar Couplings, NMR of RNA and DNA)
