Instructor:

Kathleen B. Hall

This three-credit advanced elective covers the modern solution-state NMR methods used for the study of macromolecules and their complexes. This course begins where the introductory NMR lectures in Bio 5325 and 5068 left off and assumes familiarity with the overall strategies used to solve protein structures by NMR. Emphasis is placed on understanding the powerful multidimensional NMR pulse sequences used to characterize protein and nucleic acid structure. In addition, nuclear spin relaxation as a basis for studying macromolecular dynamics is covered in depth. For a detailed syllabus, follow the link below. The reading materials will consist of papers from the primary literature and review articles, as well as the textbooks listed below. Prerequisites: either Bio 5325 or 5068 or permission from Prof. Hall. This course is intended primarily for first- and second-year graduate students in the Biochemistry, Chemical Biology, Bioorganic Chemistry, Molecular Biophysics, and Chemistry Ph.D. programs. Also, post-doctoral fellows and other scientists interested in the subject are welcomed to attend. The course is typically offered every other year and is expected to be offered again in 2010.

Textbooks:
A Handbook of Nuclear Magnetic Resonance, 2nd Edition, (1997) Ray Freeman, Addison Wesley Longman Limited, Essex, England.

Protein NMR Spectroscopy: Principles and Practice (1996) John Cavanagh, Wayne J. Fairbrother, Arthur G. Palmer III and Nicholas J. Skelton. Academic Press, San Diego, CA.

Spin Dynamics: Basics of Nuclear Magnetic Resonance, (2001), Malcom H. Levitt, John Wiley & Sons, New York, NY.