Nuclear Magnetic Resonance (NMR) spectroscopy is an important and widely used method for determination of molecular structure, and is found in diverse fields such as chemistry, biochemistry, structural biology, materials science, and medicine. NMR can be used to illustrate the basic principles of spectroscopy, quantum mechanics, and elements of electronic structure, electromagnetic theory and data processing. Examples of its applications can highlight new research in drug discovery or design of new materials.
The goal of this workshop is to provide sufficient background for the teaching of NMR theory and application, give examples of how NMR is used in research, and help provide faculty integrate NMR into their teaching. This will be done using a combination of lectures to cover theory, laboratory sessions with demonstrations and opportunities for hands-on activities, as well as supplemental lectures covering new areas of application and research. Emphasis is placed on how material can be integrated into basic chemistry and biochemistry courses.
The course is taught alternately at 2 different sites and there are some differences in content – please see below for course outlines at each site. Both locations are well equipped with spectrometers and computer workstations for the laboratory exercises.
University of Georgia, Complex Carbohydrate Research Center, Athens, GA.
Topics include:- Fundamentals of 1D and 2D NMR: generating and analyzing data; determining primary structure using homonuclear and heteronuclear data.
- Advanced solution NMR: theory of coherence, relaxation, NOE
- Applications of NMR to biomolecular systems: transferred NOE, saturation transfer difference.
- Strategies for NMR of proteins and other bio-molecules: isotope enrichment, backbone assignments, triple-resonance
- Analytical and metabolic NMR
Washington University, Center for NMR Spectroscopy, Pullman, WA
Day 1: 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.