By G.M. Clore, A.M. Gronenborn
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Additional resources for NMR of Proteins
The oldest 20 NMR pulse scheme, in which magnetization is transferred from one proton to another via IH-IH J coupling, is known as the COSY experiment and is probably the most popular experiment in the NMR analysis of small molecules. This experiment requires that J HH is not much smaller than the 1H resonance linewidth. This linewidth is approximately proportional to the inverse of the molecular tumbling rate and therefore increases approximately linearly with the size of the protein. For larger proteins 1H-I H J couplings are frequently smaller than the linewidth, making the COSY experiment ineffective.
111, 3997-4004 Haruyama, H. and Wuthrich, K. (1989). Conformation of recombinant desulfatohirudin in aqueous solution determined by nuclear magnetic resonance. Biochemistry, 28, 4301-4312 Havel, T. , Kurtz, I. D. and Crippen, G. M. (1983). Theory and practice of distance geometry. Bull. Math. , Clore, G. , Gronenborn, A. , Klee, C. B. and Bax, A. (1992). Solution structure of a calmodulin-target peptide complex by multi-dimensional NMR. , Kay, L. E. and Bax, A. (1990). A novel approach for sequential assignment of IH, I3C and 15N spectra of larger proteins: heteronuclear triple- Structures of Larger Proteins in Solution 31 resonance NMR spectroscopy.
And Gronenborn, A. M. (1989). Determination of the three-dimensional solution structure of the C-terminal domain of cellobiohydrolase I from Trichoderma ressei: a study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing. , Driscoll, P. , Kay, L. , Wingfieid, P. , Gronenborn, A. M. and Clore, G. M. (1989). Overcoming the overlap problem in the assignment of IH-NMR spectra of larger proteins using three-dimensional heteronuclear IH_ 15 N Hartmann-Hahn and nuclear Overhauser-multiple quantum coherence spectroscopy: application to interleukin-I~.