Fall, every three years (next offering Fall 2012)
Course Director: Professor A. Joshua Wand
A lecture-based course designed to introduce graduate students to applications of modern high-resolution multinuclear and multidimensional NMR spectroscopy to problems in structural biology. The course will first introduce classical definitions and descriptions of nuclear magnetic resonance and a convenient formalism for the analysis of advanced NMR experiments. Concepts and applications of multidimensional homonuclear 1H NMR and multidimensional heteronuclear spectroscopy of proteins and nucleic acids will be described. Resonance assignment strategies including analysis of triple resonance spectroscopy will be covered. The origin, measurement and extraction of structural restraints and their use in structure determination will be surveyed and illustrated with recent examples.
Prerequisites: Rudimentary knowledge of NMR and protein structure; Basic matrix algebra and calculus and elementary quantum mechanics
J. Cavanagh, W. J. Fairbrother, A. G. Palmer, III, N. Skelton Protein NMR Spectroscopy Academic Press, New York, 2007 2nd edition ISBN: 0121644901 (more formal/technical)
M. Levitt, Spin Dynamics: Basics of Nuclear Magnetic Resonance John Wiley & Sons, 2001; ISBN: 047148922
Examination: Periodic take-home questions/class presentations. Note, there may be a “workshop” scheduled separately during which student presentations will be made.
Sample Course Outline:
|1||Introduction / Basic concepts|
|5||Technical Details (with Dr. K. Valentine)|
|8||1H 2D & 3D Library|
|9||Sequential & MCD Assignment|
|10||Polarization Transfer / X-resolved|
|11||Triple resonance / Assignment strategy (with Prof. C. Tommos)|
|13||Large protein strategies|