Spectroscopy, four-dimensional

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... 

Builder, S.E. and W.S. Hancock Analytical and Process Chromatography in Pharmaceutical Protein Production, Chem. Eng. Progress, 42 (August 1988). Clore, G.M, and A M. Gronenbom Structures of Larger Proteins in Solution Three- and Four-Dimensional Heteronuclear NMR Spectroscopy." Science, 1390 (June 7. 1991). 

Clore, G.M. Gronenbom, A.M. (1991). Structures of larger proteins in solution Three- and four-dimensional heteronuclear NMR spectroscopy. Science 252, 1390-1399. 

In 1971, the idea of 2D NMR spectroscopy was proposed by Jeener and later implemented by Aue, Bartholdi and Ernst, who published their work in 1976.47 The first experiments, carried out mostly in the liquid phase, have unambiguously proved that 2D NMR spectra provide more information about a molecule than ID NMR spectroscopy and are especially useful in determining the structure of molecules that are too complicated to work with using ID NMR. With the progress in the methodology and software improvement, three-dimensional (3D) and four-dimensional (4D) NMR experiments were gradually introduced into the laboratory practice. Such strategy, the so-called multi-dimensional (or ND) NMR spectroscopy, has found a number of spectacular applications in the structure analysis of natural products. 

G. M. Clore, P. T. Wingfield, and A. M. Gronenborn, Biochemistry, 30,2315 (1991). High-Resolution Three-Dimensional Structure of Interleukin IB in Solution by Three- and Four-Dimensional Nuclear Magnetic Resonance Spectroscopy. 

Doslic, N., and Kiihn, O., The intramolecular hydrogen bond in malonaldehyde as seen by infrared spectroscopy. A four-dimensional model study, Z. Phys. Chem., 237, 1507-1524 (2003). 

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 7.1 J NMR have limited protein-structure elucidation to fairly small proteins. However, three- and four-dimensional melliods 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 Iwo-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, CXTfsY is not often employed, but experiments like N ()F.SY-TOrSY and I Of SY-HMOr are quite effective. In some cases, the three dimensions all represent different nuclei such as These... 

Tugarinov V, Kay LE, Ibraghimov 1, Orekhov VY (2005) High-resolution four-dimensional 1H-13C NOE spectroscopy using methyl-TROSY, sparse data acquisition, and multidimensional decomposition. J Am Chem Soc 127 2767-2775... 

Tugarinov V, Muhandiram R, Ayed A et al (2002) Four-dimensional NMR spectroscopy of a 723-residue protein chemical shift assignments and secondary structure of malate synthase G. J Am Chem Soc 124 10025-10035... 

Yang D, Kay LE (1999) TROSY triple-resonance four-dimensional NMR spectroscopy of a 46 ns tumbling protein. J Am Chem Soc 121 2571-2575... 

Hehnus JJ, Nadaud PS, Hofer N et al (2008) Determination of methyl [sup 13]C-[sup 15]N dipolar couplings in peptides and proteins by three-dimensional and four-dimensional magic-angle spinning solid-state NMR spectroscopy. J Chem Phys 128 052314... 

This inverse square relationship, which assumes a spherically symmetrical standing electron wave, is the fundamental equation of atomic spectroscopy and non-relativistic wave mechanics. In four-dimensional space-time, especially in a non-zero gravitational field, the assumption is not strictly valid and the proportionality factor may vary with n. 

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. 

The highly hindered disilene 2 did not react with white phosphorus, even under forcing conditions. With disilene 3, which is more hindered than 1 but less so than 2, the reaction with P4 was more complicated. It proceeded slowly, producing small amounts of both stereoisomers of the bicyclobutane compounds 70 and 70. The major product, however, was a more complex compound containing four phosphorus and four silicon atoms, also obtained as a mixture of two stereoisomers. Two-dimensional 31P NMR spectroscopy established the probable structures to be 71.98... 

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