Abstract
In recent years, a wide range of Nuclear Magnetic Resonance (NMR) techniques has become available for investigating the structure of peptides and proteins in solution, and their interactions with other molecules. These powerful methods have an important role to play in furthering our knowledge of the molecular basis of such processes as protein folding and molecular recognition. NMR spectroscopy is uniquely positioned to investigate these problems, being one of the few techniques available for determining high-resolution structures of biomolecules in solution.
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References
Wüthrich, A (1986) NMR of Proteins and Nucleic Acids Wiley-Interscience, New York.
Croasmun W. R. and Carlson R. M. K. (eds.) (1987) Two-Dimensional NMR Spec-troscopy. Applications for Chemists and Biochemists. VCH, New York.
Oppenheimer, N. J. and James, T. L. (eds.) (1989) Nuclear magnetic resonance Part A. Spectral techniques and dynamics, in Methods in Enzymology, vol 176, Academic, San Diego.
Oppenheimer, N J and James, T. L. (eds.) (1989) Nuclear magnetic resonance. Part B. Structure and mechanism, in Methods in Enzymology, vol. 177, Academtc, San Diego
Clore G. M. and Gronenborn A. M. (1989) Determination of three-dimensional structures of proteins and nucleic acids in solution by nuclear magnetic resonance spectroscopy. CRC Crit. Rev. Biochem. Mol. 24, 479–564
Fesik S. W. (1991) NMR studies of molecular complexes as a tool m drug design. J. Med Chem. 34, 2937–2945.
Derome, A. E. (1987) Modern NMR Techniques for Chemistry Research. Pergamon, Oxford.
Homans S. W. (1992) A Dictionary of Concepts in NMR. Clarendon, Oxford.
Wilthrich, A (1976) NMR in Biological Research: Peptides and Proteins. North-Holland Publishing, Amsterdam.
Ernst, R. R., Bodenhausen, G., and Wokaun, A. (1987) Principles of Nuclear Magnetic Resonance in One and Two Dimensions. Clarendon, Oxford.
Dyson, H. J. and Wright, P. E. (1991) Defining solution conformations of small linear peptides. Annu Rev. Biophys. Chem. 20, 519–538
Clore, G. M. and Gronenborn, A. M. (1991) Applications of three-and four-dimensional heteronuclear NMR spectroscopy to protein structure determination. Prog NMR Spectroscopy 23, 43–92.
Oppenheimer, N. J. (1989) Sample preparation. Meth. Enzymol. 176, 78–89
Brown, L. R. and Wtithrich, A (1981) Melittin bound to dodecylphosphocholine micelles 1H-NMR assignments and global conformational features. Biochim. Biophys. Actu 647, 95–111.
Mehlkopf, A. F., Korbee, D., Tiggelman, T. A., and Freeman, R. (1984) Sources of ti noise in two-dimensional NMR. J. Magn. Reson. 58, 315–323.
Anglister, J., Grzesiek, S., Ren, H., Klee, C.B., and Bax, A. (1993) Isotope-edited multidimensional NMR of calcineurin B in the presence of the non-deuterated detergent CHAPS. J. Biomol. NMR 3, 121–126.
Morris, G. A. (1992) Systematic sources of signal irreproducibihty and t1 noise in high-field NMR spectrometers. J. Mugn. Reson. 100, 316–328
Marion, D. and Bax, A. (1988) Baseline distortion in real Fourier transform NMR spectra. J. Magn. Reson. 79, 352–356.
Hoult, D. I., Chen, C.-N., Eden, H., and Eden, M. (1983) Elimination of baseline artifacts in spectra and their integrals. J. Mugn. Resort. 51, 110–117.
Conover, W. W. (1984) Practical guide to shimming superconducting NMR magnets, in Topics in Carbon-13 NMR Spectroscopy, vol. 4 (Levy, G., ed.), Wiley, New York, pp, 37–57.
Zuiderweg, E. R. P., Hallenga, K., and Olejniczak, E. T. (1986) Improvement of 2D NOE spectra of biomacromolecules in H20 solution by coherent suppression of the solvent resonance. .J. Magn. Reson. 70, 336–343.
Hore, P. J. (1989) Solvent suppression. Meth. Enzymol. 176, 64–77.
Lindon, J. and Ferrige, A. C. (1980) Digitisation and data processing in Fourier transform NMR. Prog. NMR Spectrosc. 14, 27–66.
Otting, G., Widmer, H., Wagner, G., and Wtithrich, K. (1986) Origin of t1 and t2 ridges in 2D NMR spectra and procedures for suppression. J. Mugn. Reson. 66, 187–193.
Marion, D. and Bax, A. (1989) Baseline correction of 2D FT NMR spectra using a simple linear prediction extrapolation of the time-domain data. J. Mugn. Reson. 83, 205–211.
Martin, M. L., Delpuech, J.-J., and Martin G. J. (1980) Practical NMR Spec-troscopy. Heyden, London, pp. 244–290.
Bundi, A. and Wiithrich, K. (1979) ’H-NMR parameters of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H-Gly-Gly-X-L-Ala-OH. Biopolymers 18, 285–297.
Sonnichsen, F. D, VanEyk, J. E., Hodges, R. E., and Sykes, B. D. (1992) Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using a synthetic actin peptide. Biochemistry 31, 8790–8798.
Dyson, H. J., Merutka, G., Waltho, J. P., Lerner, R. A., and Wright, P. E. (1992) Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding. I. Myohemerythrin. J. Mol. Biol. 226, 795–817.
Jardetzky, 0. and Roberts, G (1981) NMR in Molecular Biology. Academic, New York, p. 166.
McIntosh, L. P. and Dahlquist, F. W. (1990) Biosynthetic incorporation of 15N and t3C for assignment and interpretation of nuclear magnetic resonance spectra of proteins. Q. Rev. Biophys. 23, 1–38.
Kay, L. E, Clore, G. M., Bax, A., and Gronenborn, A M (1990) Four-dimensional heteronuclear triple-resonance NMR spectroscopy of interleukin-1 β in solution. Science 249, 411–414.
Bax, A., Sparks, S. W., and Torchia, D. A. (1989) Detection of insensitive nuclei. Meth. Enzymol. 176, 134–150.
Hull, W. E. and Sykes, B D (1976) Fluorine-19 nuclear magnetic resonance study of fluorotyrosine alkaline phosphatase: the influence of zinc on protem structure and a conformational change induced by phosphate binding. Biochemistry 15, 1535–1543.
Guntert, P. and Wuthrich, K. (1992) FLATT—A new procedure for htgh-quahty baseline correction of multidimensional NMR spectra. J. Mugn. Reson. 96, 403–407.
Marion, D., Ikura, K., and Bax, A. (1989) Improved solvent suppression m one and two dimensional NMR spectra by convolution of time domain data. J. Mugn. Reson. 84, 425–430.
Manoleras, N. and Norton, R. S. (1992) Spectral processing methods for the removal of tt noise and solvent artifacts from NMR spectra. J. Biomol. NMR 2, 485–494.
Zhu, G. and Bax, A. (1992) Two-dimensional linear prediction for signals truncated in both dimensions. .J. Magn. Reson. 98, 192–199.
Keeler, J. and Neuhaus, D. (1985) Comparison and evaluation of methods for two-dimensional NMR spectra with absorption mode lineshapes. J. Mugn. Reson. 63, 454–472.
Miiller, N., Ernst, R. R., and Wuthrich, K. (1986) Multiple-quantum-filtered two-dimensional correlated NMR spectroscopy of proteins. J. Am. Chem. Soc. 108, 6482–6492.
Braunschweiler, L. and Ernst, R. R. (1983) Coherence transfer by isotropic mixing: application to proton correlation spectroscopy. J. Magn. Reson. 53, 521–528.
Chazin, W. and Wright, P. E. (1987) A modified strategy for identification of 1H spin systems in proteins. Biopolymers 26, 973–977.
Pallaghy, P., Duggan, M., Pennington, M. W., and Norton, R. S (1993) Three-dimensional structure in solution of the calcium channel blocker w-con-otoxin. J. Mol. Biol. 234, 405–420.
Bax, A. and Davis, D. G. (1985) Practical aspects of two-dimensional transverse NOE spectroscopy. J Magn. Reson. 63, 207–213
Macura, S., Huang, Y., Suter, D., and Ernst, R. R. (1981) Two-dimensional chemical exchange and cross relaxatron spectroscopy of coupled nuclear spms J. Magn. Reson. 43, 259–281.
Neuhaus, D. and Williamson, M. (1989) The Nuclear Overhauser ESfect in Structural and Conformatlonal Analysw VCH, New York.
Kalk, A and Berendsen, H J. (1975) Proton magnetic relaxation and spin diffusion in proteins. J. Magn. Reson. 24, 343–366.
Havel, T. F. (1991) An evaluation of computational strategies for use m the determination of protem structure from distance constraints obtained by nuclear magnetic resonance. Prog Biophys Molec. Biol. 56, 43–78.
Nilges, M., Habazettl, J., Brunger, A. T., and Holak, T. A (1991) Relaxation matrix refinement of the solution structure of squash trypsm inhibitor. J. Mol Biol. 219, 499–510.
Wilcox, G. R., Fogh, R. H., and Norton, R. S. (1993) Refinement of the solution structure of the sea anemone neurotoxin ShI. J. Biol. Chem. 268, 24,707–24,719.
Dyson, H. J., Rance, M, Houghton, R. H., Lerner, R A., and Wright, P. E. (1988) Folding of immunogenic peptide fragments of proteins m water solution. I. Sequence requirements for the formation of a reverse turn J Mol. Biol. 201, 161–200
Cuba Foundation Symposia 161 (1991) Proceedings of the symposium on protem conformation, held Jan. 22–24, 1991, at the Cuba Foundation, London, England. John Wiley and Sons, Chichester, England.
Barbato, G., Ikura M., Kay, L. E., Pastor, R W., and Bax, A. (1992) Backbone dynamics of calmodulm studied by 15N relaxation using inverse detected two-dimensional NMR spectroscopy: the central helix is flexible. Biochemistry 31, 5269–5278.
Peng, J. W. and Wagner, G. (1992) Mapping of the spectral densities of the N—H bond motions in eglin c using heteronuclear relaxation experiments. Biochemistry 31, 8571–8586.
Wishart, D. S., Sykes, B. D., and Richards, F. M. (1992) The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry 31, 1647–1651.
Spera, S. and Bax, A. (1991) Empirical correlation between protein backbone conformation and Ca and Cl3 13C nuclear magnetic resonance chemical shifts. J. Am. Chem. Sot. 113, 5490–5492.
Morton, C. J., Simpson, R. J., and Norton, R. S. (1994) Solution structure of synthetic peptides corresponding to the c-terminal helix of interleukin-6. Eur. J. Biochem. 219, 97–107.
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© 1994 Humana Press Inc., Totowa, NJ
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Hinds, M.G., Norton, R.S. (1994). NMR Spectroscopy of Peptides and Proteins. In: Dunn, B.M., Pennington, M.W. (eds) Peptide Analysis Protocols. Methods in Molecular Biology, vol 36. Humana Press. https://doi.org/10.1385/0-89603-274-4:131
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DOI: https://doi.org/10.1385/0-89603-274-4:131
Publisher Name: Humana Press
Print ISBN: 978-0-89603-274-3
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