Four-dimensional spectroscopy protein structure determination

Oschkinat H, Muller T and Dieckmann T 1994 Protein structure determination with three- and four-dimensional spectroscopy Angew. Chem. Int. Ed. Engl. 33 277-93... 

G. M. Clore and A. M. Gronenborn, Prog. NMR Spectrosc., 23, 43 (1991). Applications of Three- and Four-Dimensional Heteronudear NMR Spectroscopy to Protein Structure Determination. 

Clore GM and Gronenborn AM (1991) Application of three- and four-dimensional heteronuclear NMR spectroscopy to protein structure determination. Progress in NMR Spectroscopy 26 43. 

GM Clore, AM Gronenborn. Determination of structures of larger proteins in solution by three- and four-dimensional heteronuclear magnetic resonance spectroscopy. In GM Clore, AM Gronenborn, eds. NMR of Proteins. Boca Raton, FL CRC Press, 1993, pp. 1-32. 

Overlapping resonances in 2D NMR have limited protein-structure elucidation to fairly small proteins. However, three- and four-dimensional methods have been developed that enable NMR spectroscopy to be further extended to larger and larger protein structures. A third dimension can be added, for example, to spread apart a H- H two-dimensional spectrum on the basis of the chemical shift of another nucleus, such as N or - C. In most three-dimensional experiments, the most effective methods for large molecules are used. Thus, COSY is not often employed, but experiments like NOESY-TOeSY and TOCSY-HMQC are quite effective. In some cases, the three dimensions all represent different nuclei such as H- C- N. These are considered variants of the HETCOR experiment. Multidimensional NMR is now capable of providing complete solution-phase structures to complement crystal structures from X-ray crystallography. Hence. NMR spectroscopy is now an important technique for determining structure.s and orientation.s of complex molecules in solution. 

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