NMR: Fundamentals and Applications
Gregory Helms (Washington State University, Center for NMR Spectroscopy )
and
James Prestegard
(University of Georgia)
Workshop website: http://tesla.ccrc.uga.edu/workshops/nsf/
Nuclear Magnetic Resonance (NMR) is a key technique for monitoring and defining molecular properties in such diverse fields such as chemistry, biochemistry, structural biology, materials science, and medicine. It is also one of the best media for illustration of basic principles of spectroscopy and data processing. Teaching faculty, particularly those in smaller colleges, often have not had the experience with either NMR theory or practice necessary for integrating this material into their courses or research. The goal of this workshop is to generate enthusiasm for the teaching of NMR theory and application, give examples of how NMR impacts on forefront areas of research, and provide faculty with the hands-on experience to effectively integrate NMR into their teaching. Application lectures will cover the use of simple one-dimensional and two-dimensional NMR experiments in the areas of biomolecular NMR. Laboratory sessions include screening for small molecule binding to protein active sites and visualization of binding sites using computer graphics. Emphasis is placed on how examples can be integrated into basic chemistry and biochemistry courses.
Day 1: The lecture-laboratory series begins with a discussion of the information content, structure and dynamics of NMR, the basics of the NMR phenomenon, a classical description of the NMR experiment and the basics of the spectrometer.
Day 2: Lectures and laboratories introduce identification of compounds by 1H and 13C NMR, spectral editing and 2D experiments (DEPT, INEPT, APT, 1H-1H COSY, TOCSY).
Day 3: Heteronuclear 2D methods are introduced (HETCOR, HMQC/HSQC and HMBC), along with discussion of decoupling for 1H detected experiments and either an introduction to NMR in the solid state or in biological systems.
Day 4: Cross Polarization, a survey of NMR in solids, and selective methods in liquids (Dipolar relaxation and the nOe; applications to protein structure determination).
Day 5: Reserved for laboratory exercises: Finding the Hartman-Hahn match, nOe methods on the liquids spectrometer; Protein binding site identification and visualization.
Both locations for this workshop are well equipped with spectrometers for the laboratory exercises, including wide-bore liquids/solids and high field solutions instruments (500 MHz at WSU, 800 MHz at UGA). Experiments at both sites are performed primarily on 300 MHz instruments which are available in many small colleges or accessible at nearby institutions.