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Chapter J2 - Experimental techniques

from Part J - Nuclear magnetic resonance

Published online by Cambridge University Press:  05 November 2012

Igor N. Serdyuk ,
Nathan R. Zaccai  and
Joseph Zaccai
Igor N. Serdyuk
Affiliation:
Institute of Protein Research, Moscow
Nathan R. Zaccai
Affiliation:
University of Bristol
Joseph Zaccai
Affiliation:
Institut de Biologie Structurale, Grenoble
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Summary

Fourier transform NMR spectroscopy

Principles

Experiments in the early years of NMR spectroscopy (1945–1970) used so-called continuous wave methods, in which the sample was irradiated with a weak, fixed amplitude, radio-frequency field (Fig. J2.1(a)). Spectra were obtained either by keeping the electromagnetic frequency fixed, while slowly sweeping the magnetic field strength, or vice versa, so as to bring spins with different chemical shifts sequentially into resonance. The 1970s were dominated by the revolutionary development of pulse Fourier spectroscopy (Fig. J2.1(b)), which paved the way for modern NMR and an unprecedented expansion of its applications. The starting point was the design of a multichannel spectrometer, which allowed the simultaneous measurement of many points of a frequency spectrum. It was soon recognised, however, that the instrumental effort became exorbitant as the number of channels increased.

Traditional continuous wave spectrometers have now been almost completely replaced by pulse Fourier instruments. The inherent advantages of greater sensitivity, high resolution and the absence of line-shape distortions contributed to make Fourier spectroscopy the preferred experimental technique in NMR.

In pulse Fourier instruments, data are invariably collected in the time domain; i.e. they are stored in the computer memory as a function of time. However, spectroscopists are interested in the frequency-domain response of a spin system since the energy differences between spin states possess characteristic resonance lines at specific frequencies.

Type
Chapter
Information
Methods in Molecular Biophysics
Structure, Dynamics, Function
 , pp. 1000 - 1038
Publisher: Cambridge University Press
Print publication year: 2007

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References

King, R. W., and Williams, K. R. (1989). The Fourier transform in chemistry, Part 2, Nuclear magnetic resonance: the single pulse experiment. J. Chem. Education, 66, A243–A248.CrossRefGoogle Scholar
Williams, K. R., and King, R. W. (1990). The Fourier transform in chemistry – NMR. Part 3. Multiple-pulse experiments. J. Chem. Education, 67, A93–A99.CrossRefGoogle Scholar
Williams, K. R., and King, R. W. (1990). The Fourier transform in chemistry – NMR. Part 4. Two-dimensional methods. J. Chem. Education, 67, A125–137.CrossRefGoogle Scholar
Skoog, D. A., Holler, F. J., and Nieman, T. A. (1995). Principle of instrumental analysis. Philadelphia: Saunders College Publishing.Google Scholar
Brey, W. S. (ed.). Pulse Methods in 1D and 2D Liquid-Phase NMR (1988). San-Diego: Academic.Google Scholar
Wuthrich, K. (1986). NMR of Proteins and Nucleic Acids. New York: Wiley-Interscience.Google Scholar
Kumar, A., Ernst, R. R., and Wuthrich, K. (1980). A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton–proton cross-relaxation networks in biological macromolecules. Biochem. Biophys. Res. Commun., 95, 1–6.CrossRefGoogle ScholarPubMed
Derome, A. E. (1987). Modern NMR Techniques for Chemistry Research. New York: Pergamon.Google Scholar
Ernst, R. R., Bodenhausen, G., and Wokaun, A. (1987). Principles of Nuclear Magnetic Resonance in One and Two Dimensions. Oxford: Oxford University Press.Google Scholar
Clore, G. M., and Gronenborn, A. M. (1991). Two-, three-, and four-dimensional NMR methods for obtaining more precise three-dimensional structure of proteins in solution. Ann. Rev. Biophys. Chem., 20, 29–63.CrossRefGoogle Scholar
Prestergard, J. H. (1998). New techniques in structural NMR – anisotropic interactions. Nature Struct. Biol., 5, 517–522.CrossRefGoogle Scholar
Hansen, M. R., Mueller, L., and Pardi, A. (1998). Tunable alignment of macromolecules by filamentous phage yields dipolar coupling interaction. Nature Struct. Biol., 5, 1065–1074.CrossRefGoogle Scholar
Sanders, C. R., Hare, B. J., Howard, K. P., and Prestegard, J. H. (1994). Magnetically oriented phospholipid micelles as a tool for the study of membrane-associated molecules. Prog. Nucl. Magn. Res. Spectr., 26, 5.CrossRefGoogle Scholar
Bax, A. (2003). Weak alignment offers new NMR opportunities to study protein structure and dynamics. Protein Sci., 12, 1–16.CrossRefGoogle ScholarPubMed
Gardner, K. H., and Kay, L. E. (1998). The use 2H, 13C, 15N muldimensional NMR to study the structure and dynamics of protein. Ann. Rev. Biophys. Biomol. Struct., 27, 357–406.CrossRefGoogle Scholar
Goto, N. K., and Kay, L. E. (2000). New developments in isotope labeling strategies for protein solution NMR spectroscopy. Curr. Opin. Struct. Biol., 10, 585–592.CrossRefGoogle ScholarPubMed
Tolbert, T. J., and Williamson, J. R. (1996). Preparation of specifically deuterated RNA for NMR studies using a combination of chemical and enzymatic synthesis. JACS, 116, 7929–7940.CrossRefGoogle Scholar
Wand, A. J., Ehrhardt, M. R., and Flynn, P. F. (1998). High-resolution NMR of encapsulated proteins dissolved in low-viscosity fluids. PNAS, 95, 15299–15302.CrossRefGoogle ScholarPubMed
Flynn, P. F., and Wand, A. J. (2001). High-resolution nuclear magnetic resonance of encapsulated proteins dissolved in low viscosity fluids. Meth. Enzymol., 339, 54–70.CrossRefGoogle ScholarPubMed
King, R. W., and Williams, K. R. (1989). The Fourier transform in chemistry, Part 2, Nuclear magnetic resonance: the single pulse experiment. J. Chem. Education, 66, A243–A248.CrossRefGoogle Scholar
Williams, K. R., and King, R. W. (1990). The Fourier transform in chemistry – NMR. Part 3. Multiple-pulse experiments. J. Chem. Education, 67, A93–A99.CrossRefGoogle Scholar
Williams, K. R., and King, R. W. (1990). The Fourier transform in chemistry – NMR. Part 4. Two-dimensional methods. J. Chem. Education, 67, A125–137.CrossRefGoogle Scholar
Skoog, D. A., Holler, F. J., and Nieman, T. A. (1995). Principle of instrumental analysis. Philadelphia: Saunders College Publishing.Google Scholar
Brey, W. S. (ed.). Pulse Methods in 1D and 2D Liquid-Phase NMR (1988). San-Diego: Academic.Google Scholar
Wuthrich, K. (1986). NMR of Proteins and Nucleic Acids. New York: Wiley-Interscience.Google Scholar
Kumar, A., Ernst, R. R., and Wuthrich, K. (1980). A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton–proton cross-relaxation networks in biological macromolecules. Biochem. Biophys. Res. Commun., 95, 1–6.CrossRefGoogle ScholarPubMed
Derome, A. E. (1987). Modern NMR Techniques for Chemistry Research. New York: Pergamon.Google Scholar
Ernst, R. R., Bodenhausen, G., and Wokaun, A. (1987). Principles of Nuclear Magnetic Resonance in One and Two Dimensions. Oxford: Oxford University Press.Google Scholar
Clore, G. M., and Gronenborn, A. M. (1991). Two-, three-, and four-dimensional NMR methods for obtaining more precise three-dimensional structure of proteins in solution. Ann. Rev. Biophys. Chem., 20, 29–63.CrossRefGoogle Scholar
Prestergard, J. H. (1998). New techniques in structural NMR – anisotropic interactions. Nature Struct. Biol., 5, 517–522.CrossRefGoogle Scholar
Hansen, M. R., Mueller, L., and Pardi, A. (1998). Tunable alignment of macromolecules by filamentous phage yields dipolar coupling interaction. Nature Struct. Biol., 5, 1065–1074.CrossRefGoogle Scholar
Sanders, C. R., Hare, B. J., Howard, K. P., and Prestegard, J. H. (1994). Magnetically oriented phospholipid micelles as a tool for the study of membrane-associated molecules. Prog. Nucl. Magn. Res. Spectr., 26, 5.CrossRefGoogle Scholar
Bax, A. (2003). Weak alignment offers new NMR opportunities to study protein structure and dynamics. Protein Sci., 12, 1–16.CrossRefGoogle ScholarPubMed
Gardner, K. H., and Kay, L. E. (1998). The use 2H, 13C, 15N muldimensional NMR to study the structure and dynamics of protein. Ann. Rev. Biophys. Biomol. Struct., 27, 357–406.CrossRefGoogle Scholar
Goto, N. K., and Kay, L. E. (2000). New developments in isotope labeling strategies for protein solution NMR spectroscopy. Curr. Opin. Struct. Biol., 10, 585–592.CrossRefGoogle ScholarPubMed
Tolbert, T. J., and Williamson, J. R. (1996). Preparation of specifically deuterated RNA for NMR studies using a combination of chemical and enzymatic synthesis. JACS, 116, 7929–7940.CrossRefGoogle Scholar
Wand, A. J., Ehrhardt, M. R., and Flynn, P. F. (1998). High-resolution NMR of encapsulated proteins dissolved in low-viscosity fluids. PNAS, 95, 15299–15302.CrossRefGoogle ScholarPubMed
Flynn, P. F., and Wand, A. J. (2001). High-resolution nuclear magnetic resonance of encapsulated proteins dissolved in low viscosity fluids. Meth. Enzymol., 339, 54–70.CrossRefGoogle ScholarPubMed

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