Abstract
This chapter is an overview of the current data processing capabilities of multidimensional NMR spectroscopy, a diversified area where there is a coexistence of commercial software from large multifunctional companies, small software developers, academic developments, and routines written in-house. Multidimensional NMR has been characterized by ideas and practical developments preceding commercial software tools. Two-dimensional (2D) NMR (1–4) progressed slowly initially, as it was significantly limited by existing computer technology. Impressive development took place in the 1980s (5–13) leading to the appearance of more than 2D experiments, e.g., 3D (14–19), and about 6 yr ago, 4D applications (20–22). Hardware developments, such as multiple-channel capabilities, increasing field strength, and digital technology, have enhanced the capabilities of NMR, as have isotope labeling techniques and gradient applications (23). Developments in experimental methodology (24), data processing, and data analysis (25) have made multidimensional NMR spectroscopy widely used in chemistry and materials science (26), and an equal partner to X-ray methods in studying biomolecular structure, function, and dynamics (19,27–32).
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References
Jeener, J. (1971) Pulse Pair Techniques in High Resolution NMR Ampére International Summer School, Basko Polje, Yugoslavia.
Ernst, R. R. (1975) Two-dimensional spectroscopy. Chimia 29, 179–183.
Aue, W. P., Bartholdi, E., and Ernst, R. R. (1976) Two-dimensional spectroscopy Application to nuclear magnetic resonance J. Chem. Phys. 64, 2229–2246.
Freeman, R. and Morris, G. A. (1979) Two-dimensional Fourier transformation in NMR. Bull. Magn. Reson. 1, 5–26.
Bax, A. (1984) Two-Dimensional Nuclear Magnetic Resonance in Liquids, Delft University Press/D. Reidel, Dordrecht, Holland.
Ernst, R. R., Bodenhausen, G., and Wokaun, A. (1990) Principles of Nuclear Magnetic Resonance in One and Two Dimensions, Clarendon, Oxford.
Ernst, R. R. (1987) Two-dimensional NMR spectroscopy: A powerful tool for the investigation of molecular structure and dynamics. Chimia 41, 323–340.
Morris, G. A. (1986) Modern NMR techniques for structure elucidation. Magn. Reson. Chem. 24, 371–403.
Freeman, R. (1987) A Handbook of Nuclear Magnetic Resonance, Longman (Wiley), New York.
Kessler, K., Gehrke, M., and Griesinger, C. (1988) Two-dimensional NMR spectroscopy. Background and overview of the experiments. Angew. Chem. Int. Ed. Engl. 27, 490–536.
Turner, D. L. (1985) Basic two-dimensional NMR. Prog. NMR Spectrosc. 17, 281–357.
Sanders, J. K. M. and Hunter, B. K. (1993) Modern NMR Spectroscopy: A Guide for Chemists, 2nd ed. Oxford University Press, Oxford.
Neuhaus, D. and Williamson, M. P. (1987) The Nuclear Overhauser Effect in Structural and Conformational Analysis. VCH Publishers, New York.
Griesinger, C., Serensen, O. W., and Ernst, R. R. (1989) Three-dimensional Fourier spectroscopy Application to high-resolution NMR. J. Magn. Reson. 84, 14–63.
Oschkinat, H., Cieslar, C., Holak, T., Clore, G. M., and Gronenborn, A. M. (1989) Practical and theoretical aspects of three-dimensional homonuclear Hartmann-Hahn-nuclear Overhauser enhancement spectroscopy of proteins. J. Magn. Reson. 83, 450–472.
Fesik, S. W. and Zuiderweg, E. R. P. (1990) Heteronuclear 3D NMR spectroscopy of isotopically labelled biological macromolecules. Quart. Rev. Biophys. 23, 97–131.
Wagner, G. (1990) NMR investigations of protein structure. Prog. NMR Spectrosc. 22, 101–139.
Kay, L. E., Marton, D., and Bax, A. (1989) Practical aspects of 3D heteronuclear NMR of proteins. J. Magn. Reson. 84, 72–84.
Ernst, R. R. (1992) Nuclear magnetic resonance Fourier transform spectroscopy. Angew. Chem. Int. Ed. Engl. 31, 805–823.
Kay, L. E., Clore, G. M., Bax, A., and Gronenborn, A. M. (1990) Four-dimensional heteronuclear triple-resonance NMR spectroscopy of interleukin-1 m. solution. Science 249, 411–414.
Zuiderweg, E. R. P., Petros, A. M., Fesik, S. W., and Olejniczak, E. T. (1991) Four-dimensional [13C, 1H, 13C, 1H] HMQC-NOE-HMQC NMR spectroscopy: Resolving tertiary NOE distance constraints in the spectra of larger proteins. J. Am. Chem. Soc. 113, 370–372.
Clore, G. M. and Gronenborn, A. M. (1991) Applications of three-and four-dimensional heteronuclear NMR spectroscopy to protein structure determination. Prog. NMR Spectrosc. 23, 43–92.
Keeler, J., Clowes, R. T., Davis, A. L., and Laue, E. D. (1994) Pulsed-field gradients: Theory and practice. Meth. Enzymol. 239, 145–207.
Bax, A. and Grzesiek, S. (1993) Methodological advances in protein NMR. Acc. Chem. Res. 26, 131–138.
Pelczer, I. and Szalma, S. (1991) Multidimensional NMR and data processing. Chem. Rev. 91, 1507–1524.
See publications in the special volume: (1991) Chem. Rev. 7, 1305–1624.
Oppenheimer, N. J. and James, T. L. (eds.) Methods in Enzymology, (1989) vols. 176 and 177, (1994) vol. 239. Academic, San Diego, CA.
Wagner, G. (1993) Prospects for NMR of large proteins. J. Biomol. NMR 3, 375–385.
Roberts, G. C. K. (ed.) (1993) NMR of Macromolecules. A Practical Approach. Oxford University Press, Oxford.
Clore, G. M. and Gronenborn, A. M. (eds.) (1993) NMR of Proteins. CRC, Boca Raton, FL.
Croasmun, W. R. and Carlson, R. M. (1994) Two-Dimensional NMR Spectroscopy, 2nd ed., VCH Publishers, Inc., New York.
Verlinde, C. L. M. J. and Hol, W. G. J. (1994) Structure-based drug design progress, results and challenges. Structure 2, 577–587.
Delaglio, F., Grzesiek, S., Vuister, G., Zhu, G., Pfeifer, J., and Bax, A. (1994) NMRPipe: A multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277–293.
Güntert, P., Dotsch, V., Wider, G., and Wuthrich, K. (1992) Processing of multidimensional NMR data with the new software PROSA. J. Biomol. NMR 2, 619–629.
Vuister, G. W. (1991) Homonuclear Three-Dimensional NMR Spectroscopy of Biomolecules. Ph D. Thesis, Utrecht, The Netherlands.
Mujeeb, A., Bishop, K., Peterlin, B. M., Turck, C., Parslow, T. G., and James, T. L. (1994) NMR structure of a biologically active peptide containing the RNA-binding domain of HIV-1Tat. Proc. Natl. Acad. Sci. USA 91, 8248–8252.
Kjær, M., Andersen, K. V., and Poulsen, F. M. (1994) Automated and semi-automated analysis of homo-and heteronuclear multidimensional NMR spectra of proteins. The program Pronto. Meth. Enzymol. 239, 288–307.
Garrett, D. S., Powers, R., Gronenborn, A. M., and Clore, G. M. (1991) A common sense approach to peak picking in two-, three-, and four-dimensional spectra using automatic computer analysis of contour diagrams. J. Magn. Reson. 95, 214–220.
Kleywegt, G. J., Boelens, R., Cox, M., Llinas, M., and Kaptein, R. (1991) Computer-assisted assignment of 2D 1H NMR spectra of proteins. Basic algorithms and application to phoratoxin B. J. Biomol. NMR 1, 23–47.
Kraulis, P. J. (1989) ANSIG: A program for the assignment of protein 1H 2D NMR spectra by iterative computer graphics. J. Magn. Reson. 84, 627–633.
Kraulis, P. J., Domaille, P. J., Cambell-Burk, S. L., Van Aken, T., and Laue, E. D. (1994) Solution structure and dynamics of Ras p21 · GDP determined by heteronuclear three-and four-dimensional NMR spectroscopy. Biochemistry 33, 3515–3531.
Eccles, C., Guntert, P., Billeter, M., and Wüthrich, K. (1991) Efficient analysis of protein 2D NMR spectra using the software package EASY. J. Biomol. NMR 1, 111–130.
Johnson, B. and Blevins, R. A. (1994) NMRView: A computer program for the visualization and analysis of NMR data. J. Biomol. NMR 4, 603–614.
Gooley, P. R., Johnson, B., Marcy, A. I., Cuca, G. C., Salowe, S. P., Hagmann, W. K., Esser, C. K., and Springer, J. P. (1993) Secondary structure and zinc ligation of human recombinant short-form stromelysin by multidimensional heteronuclear NMR. Biochemistry 32, 13,098–13,108.
Morris, G. A. (1992) Systematic sources of signal irreproducibility and t 1 noise in high-field NMR spectrometers. J. Magn. Reson. 100, 316–328.
Blumich, B. (1987) White noise nonlinear system analysis in nuclear magnetic resonance spectroscopy. Prog. NMR Spectrosc. 19, 331–417.
Paff, J., Freeman, R., and Blümich, B. (1993) Reduction of systematic noise in stochastic-excitation NMR by oversampling. J. Magn. Reson. Ser. A 102, 332–343.
Szalma, S., Pelczer, I., Borer, P. N., and Levy, G. C. (1993) Selective discrete Fourier transformation. An alternative approach for multidimensional NMR data processing. J. Magn. Reson. 91, 194–198.
Kaiser, R. (1974) Application of the Hadamard transform to NMR spectrometry with pseudonoise excitation. J. Magn. Reson. 15, 44–63.
Nussbaumer, H. J. and Quandalle, P. (1979) Fast computation of discrete Fourier transforms using polynomial transforms. IEEE Trans. Acoust., Speech, Signal Processing, ASSP-27, 169–181.
McGilton, H. and Morgan, R. (1983) Introducing the UNIX System, McGraw-Hill, New York.
Pelczer, I., Hoch, J. C., Roggenbuck, M. W., Valdyanathan, A., Leccarde, M. G., and Borer, P. N. (1992) Z-ANT processing; A new alternative for multidimensional NMR data processing. Poster at 33rd ENC, Pacific Grove, CA, March 29–-April 2, abstracts: WP 188.
Bishop, K. D., Pelczer, I., and James, T. L. (1993) States-Redfield phase incrementation: An alternative acquisition scheme in multidimensional NMR. Poster at 34th ENC, St. Louis, MO, March 14–18, P. 53.
Pelczer, I., Roggenbuck, M. W., Szafranski, M. S., and Spronk, C. (1994) Time domain manipulations in multidimensional NMR data processing. Lecture at Advanced School on NMR in Biology and Medicine: “NMR inside biology: from models to in vivo,” Altavilla Militia (Palermo), Italy, Sept 21–30.
Bishop, K. D., Spronk, C., Pelczer, I., and James, T. L., in preparation.
Macur, A. G., Pelczer, I., and Lysakowski, R. (1993) A proposed standard for NMR data: ADISS NMR data dictionary development and testing status. Poster at 34th ENC, St. Louis, MO, March 14–18, #227.
Macur, A. G., private communication.
McDonald, R. S. and Wilks, P. A., Jr. (1988) JCAMP-DX: A standard form for exchange of infrared spectra in computer readable form. Appl. Spectrosc. 42, 151–162.
Lysakowski, R. (1992) ASTM Standardization News, March, pp. 44–51.
NMRZ User Guide (1992) (NMRi/Tripos Associates, Inc.).
Triad NMR Advanced, User Guide (1993) (Tripos Associates, Inc./NMRi).
Keeler, J. and Neuhaus, D. (1985) Comparison and evaluation of methods for two-dimensional NMR spectra with absorption-mode lineshapes. J. Magn. Reson. 63, 454–472.
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. Magn. Reson. 83, 205–211.
Kay, L. E., Ikura, M., Zhu, G., and Bax, A. (1991) Four-dimensional heteronuclear triple-resonance NMR of isotopically enriched proteins for sequential assignment of backbone atoms. J. Magn. Reson. 91, 422–428.
Ikura, M., Bax, A., Clore, M. G., and Gronenborn, A. M. (1990) Detection of nuclear Overhauser effects between degenerate amide proton resonances by heteronuclear three-dimensional nuclear magnetic resonance spectroscopy. J. Am. Chem. Soc. 112, 9020–9022.
Ernst, R. R. (1969) Numerical Hilbert transform and automatic phase correction in magnetic resonance spectroscopy. J. Magn. Reson. 1, 7–26.
Zolnai, Zs., Macura, S., and Markley, J. L. (1990) Phasing two-and three-dimensional NMR spectra by use of the Hilbert transform can save computer time and space. J. Magn. Reson. 89, 94–101.
Press, W. H., Flannery, B. P., Teukolsky, S. A., and Vetterling, W. T. (1987) Numerical Recipes. The Art of Scientific Computing, Cambridge University Press, Cambridge, UK.
Bodenhausen, G., Kogler, H., and Ernst, R. R. (1984) Selection of coherence-transfer pathways in NMR pulse experiments. J. Magn. Reson. 58, 370–388.
Bax, A. (1985) A simple description of two-dimensional NMR spectroscopy. Bull. Magn. Reson. 7, 167–183.
Nagayama, K. (1986) Four-quadrant pure-phase representation of two-dimensional spectra with time-reversal or frequency inversion. J. Magn. Reson. 66, 240–249.
Bachmann, P., Aue, W. P., Muller, L., and Ernst, R. R. (1977) Phase separation in two-dimensional spectroscopy. J. Magn. Reson. 28, 29–39.
Turner, D. L. (1986) The application of time reversal to the generation of pure absorption lineshapes in heteronuclear shift-correlation spectra. J. Magn. Reson. 70, 465–471.
Williamson, M. P. (1983) Pure absorption phase proton 2D J-resolved spectroscopy. J. Magn. Reson. 55, 471–474.
Titman, J. J., Luz, Z., and Spiess, H. W. (1992) Solid-state reactions studied by carbon-13 rotor-synchronized magic angle spinning two-dimensional exchange NMR 1. Self-diffusion and the tautomeric hydrogen shift in tropolone. J. Am. Chem. Soc. 114, 3756–3765.
States, D. J., Haberkorn, R. A., and Ruben, D. J. (1982) A two-dimensional nuclear Overhauser experiment with pure absorption phase in four quadrants. J. Magn. Reson. 48, 286–292.
Drobny, G., Pines, A., Sinton, S., Weitekamp, D., and Wemmer, D. (1979) Fourier transform multiple quantum nuclear magnetic resonance. Faraday Div. Chem. Soc. Symp. 13, 49–55.
Marion, D. and Wuthrich, K. (1983) Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling in proteins. Biochem. Biophys. Chem. Commun. 113, 967–974.
Redfield, A. G. and Kunz, S. D. (1975) Quadrature Fourier NMR detection. Simple multiplex and discussion. J. Magn. Reson. 19, 250–254.
Marion, D., Ikura, M., Tschudin, R., and Bax, A. (1989) Rapid recording of 2D NMR spectra without phase cycling. Application to the study of hydrogen exchange in proteins. J. Magn. Reson. 85, 393–399.
Muller, L., and Ernst, R. R. (1979) Coherence transfer in the rotating frame Application to heteronuclear cross-correlation spectroscopy. Mol. Phys. 38, 963–992.
Bax, A., Ikura, M., Kay, L. E., and Zhu, G. (1991) Removal of F1 baseline distortion and optimization of folding in multidimensional NMR spectra. J. Magn. Reson. 91, 174–178.
Archer, S. J., Baldisseri, D. M., and Torchia, D. A. (1992) Optimization of baseline and folding in spectra obtained using the TPPI format. J. Magn. Reson. 97, 602–606.
Marion, D. and Bax, A. (1988) Baseline distortions in real-Fourier-transform NMR spectra. J. Magn. Reson. 79, 352–356.
Schmieder, P., Zimmer, S., and Kessler, H. (1991) Increased resolution in proton detected heteronuclear NMR experiments by folding in the hetero-dimension. Magn. Reson. Chem. 29, 375–380.
Rance, M., Chazin, W. J., Dalvit, C., and Wright, P. E. (1989) Multiple-quantum nuclear magnetic resonance. Meth. Enzymol. 176, 114–134.
Pelczer, I. and Bishop, K. D., in preparation.
Borer, P. N., Lin, Y., Wang, S., Roggenbuck, M. W., Gott, J. M., Uhlenbeck, O. C., and Pelczer, I. (1995) Proton NMR and structural features of a 24-nucleotide RNA hairpin. Biochemistry 34, 6488–6503.
Simorre, J.-P. and Marion, D. (1990) Acquisition schemes and quadrature artifacts in phase-sensitive two-dimensional NMR. J. Magn. Reson. 89, 191–197.
Bishop, K. D., Borer, P. N., and Pelczer, I. (1996) Improved proton assignment of DNA by application of aliasing and dispersive-absorptive phasing to two-quantum COSY spectra. J. Magn. Reson. Ser. B 110, 9–15.
Led, J. J. and Gesmar, H. (1991) Application of the linear prediction method to NMR spectroscopy. Chem. Rev. 7, 1413–1426.
Zhu, G. and Bax, A. (1990) Improved linear prediction for truncated signals of known phase. J. Magn. Reson. 90, 405–410.
Zhu, G. and Bax, A. (1992) Two-dimensional linear prediction for signals truncated in both dimensions. J. Magn. Reson. 98, 192–199.
Pelczer, I. and Roggenbuck, M. W. (1993) Clean homonuclear correlation spectra through combined time and frequency domain data processing. Poster at 1993 Eastern Analytical Symposium, Somerset, NJ, Nov. 14–19, #353.
Delsuc, M. A. and Lallemand, J. Y. (1986) Improvement of dynamic range in NMR by oversampling. J. Magn. Reson. 69, 504–507.
Fukushima, E. and Roeder, S. B. W. (1981) Experimental Pulse NMR: A Nuts and Bolts Approach, Addison-Wesley, Reading, MA.
Cory, D. G., Garroway, A. N., and Miller, J. B. (1990) Improved resolution of multiple-pulse proton images by oversamphng. J. Magn. Reson. 87, 202–207.
Wider, G. (1990) Elimination of baseline artifacts in NMR spectra by oversampling. J. Magn. Reson. 89, 406–409.
Waltho, J. P. and Cavanagh, J. (1993) Practical aspects of recording multidimensional NMR spectra in water with flat baselines. J. Magn. Reson., Ser. A 103, 338–348.
Rance, M. and Byrd, A. (1983) Obtaining high-fidelity spin-1/2 powder spectra in anisotropic media: Phase cycled Hahn-echo spectrosocpy. J. Magn. Reson. 52, 221–240.
Davis, D. G. (1989) Elimination of baseline distortions and minimization of artifacts from phased 2D NMR spectra. J. Magn. Reson. 81, 603–607.
Kurihara, N., Kamo, O., Umeda, M., Sato, K., Hyakuna, K., and Nagayama, K. (1985) Applications in one-dimensional and two-dimensional NMR of a pseudofilter by jittered averaging. J. Magn. Reson. 65, 405–416.
Kumar, A., Brown, S. C., Donlan, M. E., Meier, B. U., and Jeffs, P. W. (1991) Optimization of two-dimensional NMR by matched accumulation. J. Magn. Reson. 95, 1–9.
Bax, A., Griffey, R. H., and Hawkins, B. L. (1983) Sensitivity-enhanced correlation of 15N and 1H chemical shifts in natural abundance samples via multiple quantum coherence. J. Am. Chem. Soc. 105, 7188–7190.
Sørensen, O. W. and Ernst, R. R. (1983) Remote heteronuclear correlation via pseudo multiple quantum spectroscopy. J. Magn. Reson. 55, 338–343.
Ramachandran, R., Darba, P., and Brown, L. R. (1988) Selection of coherence pathways by Fourier analysis. Application to multiple quantum spectroscopy. J. Magn. Reson. 78, 56–68.
Wider, G., Neri, D., and Wüthrich, K. (1991) Studies of slow conformational equilibria in macromolecules by exchange of heteronuclear longitudinal 2-spin-order in a 2D difference correlation experiment. J. Biomol. NMR 1, 93–98.
Otting, G., Liepinsh, E., and Wüthrich, K. (1993) Disulfide bond isomerization in BPTI and BPTI(G36S): An NMR study of correlated mobility in proteins. Biochemistry 32, 3571–3582.
Otting, G. and Wüthrich, K. (1989) Extended heteronuclear editing of 2D 1H NMR spectra of isotope-labeled proteins, using the X(ω1, ω2) double half filter. J. Magn. Reson. 85, 586–594.
Wider, G., Weber, C., Traber, R., Widmer, H., and Wüthrich, K. (1990) Use of double-half-filter in two-dimensional 1H NMR nuclear magnetic resonance studies of receptor-bound cyclosporin. J. Am. Chem. Soc. 112, 9015–9016.
Fesik, S. W., Gampe, Jr., R. T., Eaton, H. L., Gemmecker, G., Olejniczak, E. T., Neri, P., Holzman, T. F., Egan, D. A., Edalji, R., Simmer, R., Helfrich, R., Hochlowski, J., and Jackson, M. (1991) NMR studies of [U-13C]cyclosporin A bound to cyclophylin: Bound conformation and portions of cyclosporin involved in binding. Biochemistry 30, 6574–6583.
Farmer, B. T., II and Mueller, L. (1994) Simultaneous acquisition of [13C, 15N]− and [15N, 15N]− separated 4D gradient-enhanced NOESY spectra in proteins. J. Biomol. NMR 4, 673–687.
Pelczer, I. (1993) Simple COSY applications. Lecture at the 1993 Eastern Analytical Symposium, Somerset, NJ, Nov. 14–19, abstracts #88.
Cavanagh, J. and Rance, M. (1990) Sensitivity improvement in isotropic mixing (TOCSY) experiments. J. Magn. Reson. 88, 72–85.
Linehart, J. and Pelczer, I. (1993) FOP, a simple UNIX routine for linear combination of multidimensional NMR data. Chemistry Department, Syracuse University (available on request).
Brigham, E. O. (1974) The Fast Fourier Transform, Prentice-Hall, London.
Barna, J. C. J., Laue, E. D., Mayger, M. R., Skilling, J., and Worrall, S. J. P. (1986) Reconstruction of phase-sensitive two-dimensional nuclear-magnetic-resonance spectra using maximum entropy. Biochem. Soc. Trans. 14, 1262–1263.
Barna, J. C. J., Laue, E. D., Mayger, M. R., Skilling, J., and Worrall, S. J. P. (1987) Exponential sampling, an alternative method for sampling in two-dimensional NMR experiments. J. Magn. Reson. 73, 69–77.
Barna, J. C. J. and Laue, E. D. (1987) Conventional and exponential sampling for 2D NMR experiments with application to a 2D NMR spectrum of a protein. J. Magn. Reson. 75, 384–389.
Bax, A., Mehlkopf, A. F., and Smidt, J. (1979) Homonuclear broadband-decoupled absorption spectra, with linewidths which are independent of the transverse relaxation rate. J. Magn. Reson. 35, 167–169.
Rance, M., Wagner, G., Sørensen, O. W., Wüthrich, K., and Ernst, R. R. (1984) Application of ω1-decoupled 2D correlation spectra to the study of proteins. J. Magn. Reson. 59, 250–261.
Ikura, M., Kay, L. E., and Bax, A. (1991) Improved three-dimensional 1H-13C-1H correlation spectroscopy of a 13C-labeled protein using constant-time evolution. J. Biomol. NMR 1, 299–304.
Vuister, G. W. and Bax, A. (1992) Resolution enhancement and spectral editing of uniformly 13C-enriched proteins by homonuclear broadband 13C decoupling. J. Magn. Reson. 98, 428–435.
Kay, L. E., Wittekind, M., McCoy, M. A., Friedrichs, M. S., and Mueller, L. (1992) 4D NMR Triple-resonance experiments for assignment of protein backbone nuclei using shared constant-time evolution periods. J. Magn. Reson. 98, 443–450.
Schmieder, P., Stern, A. S., Wagner, G., and Hoch, J. C. (1993) Application of nonlinear sampling schemes to COSY-type spectra. J. Biomol. NMR 3, 569–576.
Schmieder, P., Stern, A. S., Wagner, G., and Hoch, J. C. (1994) Improved resolution in triple-resonance spectra by nonlinear sampling in the constant-time domain. J. Biomol. NMR 4, 483–490.
Markus, M. A., Nakayama, T., Matsudaira, P., and Wagner, G. (1994) 1H, 15N, 13C and 13CO resonance assignments and secondary structure of villin 14T, a domain conserved among actin-severing proteins. J. Biomol. NMR 4, 553–574.
Lindon, J. C. and Ferrige, A. G. (1980) Digitisation and data processing in Fourier transform NMR. Prog. NMR Spectrosc. 14, 27–66.
Derome, A. E. (1987) Modern NMR Techniques for Chemistry Research, Pergamon, Oxford.
Hoult, D. I., Chen, C.-N., Eden, H., and Eden, M. (1983) Elimination of baseline artifacts in spectra and their integrals. J. Magn. Reson. 51, 111–117.
Heuer, A. and Haeberlen, U. (1989) A new method for suppressing baseline distortions in FT NMR. J. Magn. Reson. 85, 79–94.
Otting, G., Wider, H., Wagner, G., and Wuthrich, K. (1986) Origin of t 1 and t 2 ridges in 2D NMR spectra and procedures for suppression. J. Magn. Reson. 66, 187–193.
Zhu, G., Torchia, D., and Bax, A. (1993) Discrete Fourier transformation of NMR signals. The relationship between sampling delay time and spectral baseline. J. Magn. Reson., Ser. A 105, 219–222.
Starcuk, Z., Jr., Bartusek, K., and Starcuk, Z. (1994) First-data-point problem and the baseline distortion in Fourier-transform NMR spectroscopy with simultaneous sampling. J. Magn. Reson., Ser A 108, 177–188.
Henrichs, P. M., Hewitt, J. M., and Young, R. H. (1986) Baseline roll and phase distortion of NMR spectra. An algorithm for the generation of reliable powder spectra of solids. J. Magn. Reson. 69, 460–466.
Thériault, Y., Pochapsky, T. C., Dalvit, C., Ciu, M. L., Sligar, S. G., and Wright, P. E. (1994) 1H and 15 resonance assignments and secondary structure of the carbon monoxide complex of sperm whale myoglobin. J. Biomol. NMR 4, 491–504.
Starcuk, Z., Starcuk, Z., Jr., and Halámek, J. (1990) Correction of baseline and lineshape distortions in Fourier transform NMR spectroscopy by estimation of missing signals. J. Magn. Reson. 86, 30–38.
Stephenson, D. S. (1988) Linear prediction and maximum entropy methods in NMR spectroscopy. Prog. NMR Spectrosc. 20, 515–626.
Ross, A., Czisch, M., Cieslar, C., and Holak, T. A. (1993) Efficient methods for obtaining phase-sensitive gradient-enhanced HMQC spectra. J. Biomol. NMR 3, 215–224.
Wang, K. Y., Swaminathan, S., and Bolton, P. H. (1994) Tertiary structure motif of Oxytricha telomere DNA. Biochemistry 33, 7517–7527.
Ni, F., Ripoll, D. R., and Purisima, E. O. (1992) Conformational stability of a thrombin-binding peptide derived from the hirudin C-terminus. Biochemistry 31, 2545–2554.
Smallcombe, S. H. (1993) Solvent suppression with symmetrically-shifted pulses. J. Am. Chem. Soc. 115, 4776–4785.
Bothner-By, A. A. and Dadok, J. (1987) Useful manipulations of the free induction decay. J. Magn. Reson. 72, 540–543.
Rexroth, A., Szalma, S., Weisemann, R., Bermel, W., Schwalbe, H., and Griesinger, C. (1994) Determination of 3J(H1N,C′1) coupling constants in proteins with the C′-FIDS method. J. Biomol. NMR 6, 237–244.
Nagayama, K., Kumar, A., Wuthrich, K., and Ernst, R. R. (1980) Experimental techniques of two-dimensional correlated spectroscopy. J. Magn. Reson. 40, 321–334.
Wider, G., Macura, S., Kumar, A., Ernst, R. R., and Wuthrich, K. (1984) Homonuclear two-dimensional 1H NMR of proteins. Experimental procedures. J. Magn. Reson. 56, 207–234.
Macura, S. and Brown, L. R. (1983) Improved sensitivity and resolution in two-dimensional homonuclear J-resolved NMR spectroscopy of macromolecules. J. Magn. Reson. 53, 529–535.
Macura, S. and Brown, L. R. (1985) Heteronuclear two-dimensional J-resolved spectroscopy of macromolecules. J. Magn. Reson. 62, 328–335.
Muller, L. (1979) High-sensitivity two-dimensional carbon-13 spectroscopy. J. Magn. Reson. 36, 301–309.
Brownstein, S. and Bornais, J. (1982) Unfolding of two-dimensional spectra which are folded in the f 1 dimension. J. Magn. Reson. 47, 398–408.
Bax, A., Griffey, R. H., and Hawkins, B. L. (1983) Correlation of proton and nitrogen-15 chemical shifts by multiple quantum NMR. J. Magn. Reson. 55, 301–315.
Bartholdi, E. and Ernst, R. R. (1973) Fourier spectroscopy and the causality principle. J. Magn. Reson. 11, 9–19.
Wang, S. S., Pelczer, I., Borer, P. N., and Levy, G. C. (1994) Maximum likelihood deconvolution of NMR spectra in multidimensional space. J. Magn. Reson., Ser. A 108, 171–176.
Friedrichs, M. S., Metzler, W. J., and Mueller, L. (1991) Removal of diagonal peaks in two-dimensional NMR spectra by means of digital filtering. J. Magn. Reson. 95, 178–183.
Redfield, A. G. and Gupta, A. K. (1971) Pulsed Fourier-transform NMR spectrometer for use with H2O solutions. J. Chem. Phys. 54, 1418–1419.
Adler, M. and Wagner, G. (1991) Removal of dispersive baseline distortions caused by strong water signals. J. Magn. Reson. 91, 450–454.
Stockman, B. J., Nirmala, N. R., Wagner, G., Delcamp, T. J., DeYarman, M. T., and Freisheim, J. H. (1992) Sequence-specific 1H and 15N resonance assignments for human dihydrofolate reductase in solution. Biochemistry 31, 218–229.
Clubb, R. T., Thanabal, V., Osborne, C., and Wagner, G. (1991) 1H and 15N resonance assignments of oxidized flavodoxin from Anacystis nidulens with 3D NMR. Biochemistry 30, 7718–7730.
Tsang, P., Wright, P. E., and Rance, M. (1990) Signal suppression in the frequency domain to remove undesirable resonances with dispersive lineshapes. J. Magn. Reson. 88, 210–215.
Johnson, B. (1992) Baseline flattening by automatic phasing of dispersive water signals. J. Magn. Resort. 100, 189–194.
Mitschang, L., Cieslar, C., Holak, T. A., and Oschkinat, H. (1991) Application of the Karhunen-Loéve transformation to the suppression of undesired resonances in three-dimensional NMR. J. Magn. Reson. 92, 208–217.
Ahmed, N. and Rao, K. R. (1975) Orthogonal Transforms for Digital Signal Processing, Springer, Berlin.
Callaghan, P. T., MacKay, A. L., Pauls, K. P., Soderman, O., and Bloom, M. (1984) The high fidelity extraction of weak broad lines from NMR spectra containing large solvent peaks. J. Magn. Reson. 56, 101–109.
Bielecki, A. and Levitt, M. H. (1989) Frequency-selective double-quantum-filtered COSY in water. J. Magn. Reson. 82, 562–570.
Kuroda, Y., Wada, A., Yamazaki, T., and Nagayama, K. (1989) Postacquisition data processing method for suppression of the solvent signal. J. Magn. Reson. 84, 604–610.
Kuroda, Y., Wada, A., Yamazaki, T., and Nagayama, K. (1990) Postacquisition data processing method for suppression of the solvent signal. II. The weighted first derivative. J. Magn. Reson. 88, 141–145.
Marion, D., Ikura, M., and Bax, A. (1989) Improved solvent suppression in one-and two-dimensional NMR spectra by convolution of time-domain data. J. Magn. Reson. 84, 425–430.
Cross, K. J. (1993) Improved digital filtering technique for solvent suppression. J. Magn. Reson., Ser. A 101, 220–224.
Sodano, P. and Delepierre, M. (1993) Clean and efficient suppression of the water signal in multidimensional NMR spectra. J. Magn. Reson., Ser. A 104, 88–92.
Ni, F. (1992) Improved methods for solvent suppression and baseline correction in two-dimensional transferred NOE experiments. J. Magn. Reson. 99, 391–397.
Ni, F. (1992) Optimized acquisition and processing of homonuclear 3D NMR spectra. Applications to transferred-NOE experiments. J. Magn. Reson. 100, 391–400.
Pelczer, I., Sartor, G., Franzoni, L., and Spisni, A. (1994) Non-labeled large biomolecules: the challenge for NMR structural studies. Poster at the XXV Congresso Nazionale Risonanze Magnetiche, Trieste, Italy, Oct. 3–5.
Pelczer, I. (1991) Correlation spectroscopy at a bargain: SIMPLE-COSY. J. Am. Chem. Soc. 113, 3211–3212.
Mronga, S. and Balbach, J. (1992) Multiplet structure in real cosine Fourier-transformed zero-quantum spectra without axial peaks. J. Magn. Reson. 98, 421–427.
Nagayama, K., Wuthrich, K., and Ernst, R. R. (1979) Two-dimensional spin-echo correlated spectroscopy (SECSY) for 1H NMR studies of biological macromolecules. Biochem. Biophys. Res. Commun. 90, 305–311.
Bax, A. and Freeman, R. (1981) Investigation of complex networks of spin-spin coupling by two-dimensional NMR. J. Magn. Reson. 44, 542–561.
Vuister, G. W., Boelens, R., and Kaptein, R. (1988) Nonselective three-dimensional NMR spectroscopy. The 3D NOE-HOHAHA experiment. J. Magn. Reson. 80, 176–185.
Hoch, J. C. (1989) Modern spectrum analysis in nuclear magnetic resonance. Alternatives to the Fourier transform. Meth. Enzymol. 176, 216–241.
Cieslar, C., Holak, T. A., and Oschkinat, H. (1990) 3D TOCSY-TOCSY Processing using linear prediction, as a potential technique for automated assignment. J. Magn. Reson. 89, 184–190.
Grzesiek, S. and Bax, A. (1993) Amino acid type determination in the sequential assignment procedure of uniformly 13C/15N-enriched proteins. J. Biomol. NMR 3, 185–204.
Seip, S., Balbach, J., Behrens, S., Kessler, H., Flukiger, K., de Meyer, R., and Erni, B. (1994) Mannose transporter in Escherichia coli. Backbone assignments and secondary structure of the IIA domain of the IIABMan subunit. Biochemistry 33, 7174–7183.
Barkhuijsen, H., de Beer, R., Bovée, W. M. M. J., and van Ormondt, D. (1985) Retrieval of frequencies, amplitudes, damping factors, and phases from time-domain signals using a linear least-squares procedure. J. Magn. Reson. 61, 465–481.
Bagby, S., Harvey, T. S., Kay, L. E., Eagle, S. G., Inouye, S., and Ikura, M. (1994) Unusual helix-containing greek keys in development-specific Ca2+ binding protein S. 1H, 15N, and 13C assignment and secondary structure determined with the use of multidimensional double and triple resonance heteronuclear NMR spectroscopy. Biochemistry 33, 2409–2421.
Szalma, S. (1989) TRAWIATA—An efficient algorithm to decrease the transformation time of multidimensional NMR arrays. J. Magn. Reson. 83, 400–403.
Chylla, R. A. and Markley, J. L. (1993) Improved frequency resolution in multidimensional constant-time experiments by multidimensional Bayesian analysis. J. Biomol. NMR 3, 515–533.
Ikura, M., Clore, G. M., Gronenborn, A. M., Zhu, G., Klee, C. B., and Bax, A. (1992) Solution structure of a calmodulin-target peptide complex by multidimensional NMR. Science 256, 632–638.
Bax, A., Byrd, R. A., and Aszalos, A. (1984) Spin multiplet enhancement in two-dimensional correlated NMR spectroscopy. J. Am. Chem. Soc. 106, 7632–7633.
Alexandrescu, A. T., Abeygunawardana, C., and Shortle, D. (1994) Structure and dynamics of a denaturated 131-residue fragment of staphylococcal nuclease. A heteronuclear study. Biochemistry 33, 1063–1072.
Borer, P. N. and Levy, G. C. (1994) Using maximum likelihood spectral deconvolution in multidimensional nuclear magnetic resonance. Meth. Enzymol. 239, 257–288.
Liang, Z. and Marshall, A. G. (1990) Time-domain (interferogram) and frequency-domain (absorption-mode and magnitude-mode) noise and precision in Fourier transform spectroscopy. Appl. Spectrosc. 44, 766–775.
Szalma, S. and Pelczer, I. (1992) Multidimensional magnetic resonance system using selective discrete Fourier transformation (SDFT) US patent, November 17. patent number: ISBN 5,164,670.
Hore, P. J. (1985) NMR data processing using the maximum entropy method. J. Magn. Reson. 62, 561–567.
Hoch, J. C. (1985) Maximum entropy signal processing of two-dimensional NMR data. J. Magn. Reson. 64, 436–440.
Ni, F., Levy, G. C., and Scheraga, H. A. (1986) Simultaneous resolution enhancement and noise suppression in NMR signal processing by combined use of maximum entropy and Fourier self-deconvolution methods. J. Magn. Reson. 66, 385–390.
Ni, F. and Scheraga, H. A. (1989) Constrained iterative spectral deconvolution with applications in NMR spectroscopy. J. Magn. Reson. 82, 413–418.
Daniell, G. J. and Hore, P. J. (1989) Maximum entropy and NMR—A new approach. J. Magn. Reson. 84, 515–536.
Kumaresan, R., Ramalingam, C. S., and van Ormondt, D. (1990) Estimating the parameters of NMR signals by transforming to the frequency domain. J. Magn. Reson. 89, 562–567.
De Beer, R., Van Ormondt, D., Pijnappel, W. W. F., and van der Veen, J. W. C. (1988) Quantitative analysis of magnetic resonance signals in the time domain. Israel J. Chem. 28, 249–261.
Jones, J. A. and Hore, P. J. (1991) The maximum entropy method and Fourier transformation compared. J. Magn. Reson. 92, 276–292.
Jones, J. A. and Hore, P. J. (1991) The maximum entropy method. Appearance and reality. J. Magn. Reson. 92, 363–376.
Knijn, A., de Beer, R., and van Ormondt, D. (1992) Frequency-selective quantification in the time domain. J. Magn. Reson. 97, 444–450.
Yan, H., and Gore, J. C. (1990) The performance of LP-ZOOM for local spectral analysis of NMR signals. J. Magn. Reson. 88, 354–358.
Angelidis, P. A. and Sergiadis, G. D. (1993) Time-frequency representation of damped sinusoids using the Zak transform. J. Magn. Reson. Ser. A 103, 191–195.
Chen, S. C., Schaewe, T. J., Teichman, R. S., Miller, M. I., Nadel, S. N., and Greene, A. S. (1993) Parallel algorithms for maximum-likelihood nuclear magnetic resonance spectroscopy. J. Magn. Reson. Ser. A 102, 16–23.
Miller, M. I., Chen, S. C., Kuefler, D. A., and d’Avignon, D. A. (1993) Maximum likelihood and the EM algorithm for 2D NMR spectroscopy. J. Magn. Reson. Ser. A 104, 247–257.
Stern, A. S. and Hoch, J. C. (1992) A new storage-efficient algorithm for maximum-entropy spectrum-reconstruction. J. Magn. Reson. 97, 255–270.
Spera, S., Ikura, M., and Bax, A. (1991) Measurement of the exchange rates of rapidly exchanging amide protons: Application to the study of calmodulin and its complex with a myosin light chain kinase fragment. J. Biomol. NMR 1, 155–165.
Frenkiel, T., Bauer, C., Carr, M. D., Birdsall, B., and Feeney, J. (1990) HMQC-NOESY-HMQC. A three-dimensional NMR experiment which allows detection of all NOEs for a molecule while providing 15N frequency separation of degenerate amide protons. J. Magn. Reson. 90, 420–425.
Carpenter, K. A. and Ni, F. (1992) A heteronuclear 3D NMR experiment which allows detection of all NOES for a molecule while providing 15N frequency separation of degenerate amide protons. J. Magn. Reson. 99, 192–197.
Marshall, A. and Roe, D. C. (1978) Dispersion versus absorption: Spectral line shape analysis for radiofrequency and microwave spectrometry. Anal Chem. 50, 756–763.
Roe, D. C., Marshall, A. G., and Smallcombe, S. H. (1978) Dispersion versus absorption: Analysis of line-broadening mechanisms in nuclear magnetic resonance spectrometry. Anal. Chem. 50, 764–767.
Craig, E. C. and Marshall, A. G. (1988) Automated phase correction of FT NMR spectra by means of phase measurement based on dispersion versus absorption relation. J. Magn. Reson. 76, 458–475.
Hoffman, R. E., Delaglio, F., and Levy, G. C. (1992) Phase correction of two-dimensional NMR spectra using DISPA. J. Magn. Reson. 98, 231–237.
Heuer, A. (1991) A new algorithm for automatic phase correction by symmetrizing lines. J. Magn. Reson. 91, 241–253.
Gibbs, A. and Moms, G. A. (1991) Reference deconvolution. Elimination of distortions arising from reference line truncation. J. Magn. Reson. 91, 77–83.
Ikura, M. and Bax, A. (1992) Isotope-filtered 2D NMR of a protein-peptide complex: Study of a skeletal muscle myosin light chain kinase fragment bound to calmodulin. J. Am. Chem. Soc. 114, 2433–2440.
Eriksson, P.-O. and Sahlman, L. (1993) 1H NMR studies of the mercuric ion binding protein MerP: Sequential assignment, secondary structure and global fold of oxidized MerP. J. Biomol. NMR 3, 613–626.
Pelczer, I., Bishop, K. D., Levy, G. C., and Borer, P. N. (1991) Modified presentation of double quantum correlation spectra—Application to DNA oligomers. J. Magn. Reson. 91, 604–606.
Turner, D. L. (1982) Carbon-13 autocorrelation NMR using double-quantum coherence. J. Magn. Reson. 49, 175–178.
Bax, A. and Marion, D. (1988) Improved resolution and sensitivity in 1H-detected heteronuclear multiple-bond correlation spectroscopy. J. Magn. Reson. 78, 186–191.
Sklenár, V., Miyashiro, H., Zon, G., Miles, H. T., and Bax, A. (1986) Assignment of the 31P and 1H resonances in oligonucleotides by two-dimensional NMR spectroscopy. FEBS Lett. 208, 94–98.
Nagayama, K. (1986) ω1-Absorption/ω2-magnitude spectra. Mixed-mode representation in two-dimensional NMR. J. Magn. Reson. 69, 508–510.
Chandrakumar, N. and Nagayama, K. (1986) Fully automated four-quadrant pure-phase representation of two-dimensional spectra. J. Magn. Reson. 69, 535–537.
Lippens, G. and Hallenga, K. (1990) Perfectly flat baselines in 1D and 2D spectra with optimized spin-echo detection. J. Magn. Reson. 88, 619–626.
Frøystein, N. Å. (1993) Removal of all baseline and phase distortions from 2D NOE spectra by tailored spin-echo evolution and detection. J. Magn. Reson. Ser. A 103, 332–337.
Heus, H. A. and Pardi, A. (1991) Novel 1H nuclear magnetic resonance assignment procedure for DNA duplexes. J. Am. Chem. Soc. 113, 4360–4361.
Rouh, A., Delsuc, M.-A., Bertrand, G., and Lallemand, J.-Y. (1993) The use of classification in baseline correction of FT NMR spectra. J. Magn. Reson. Ser. A 102, 357–359.
Chylla, R. A. and Markley, J. L. (1993) Simultaneous basepoint correction and signal recognition in multidimensional NMR spectra. J. Magn. Reson. Ser. B 102, 148–154.
Güntert, P. and Wüthrich, K. (1992) FLATT—A new procedure for high-quality baseline correction of multidimensional NMR spectra. J. Magn. Reson. 96, 403–407.
Saeed, N. and Menon, D. K. (1993) A knowledge-based approach to minimize baseline roll in chemical shift imaging. Magn. Reson. Med. 29, 591–598.
Zolnai, Zs., Macura, S., and Markley, J. L. (1989) Spline method for correcting baseplane distortions in two-dimensional NMR spectra. J. Magn. Reson. 82, 496–504.
Levy, G. C., Pelczer, I., Jeong, G.-W., and Wang, K. (1993) Totally automated two dimensional baseplane correction. J. Magn. Reson. Ser. A 105, 316–320.
Rinaldi, P. L. and Iverson, D. J. (1991) A new method of 2D NMR data collection for time saving and artifact reduction. J. Magn. Reson. 92, 528–537.
Derome, A. E. and Williamson, M. P. (1990) Rapid pulsing artifacts in double-quantum-filtered COSY. J. Magn. Reson. 88, 177–185.
Turner, C. J. and Hutton, W. C. (1992) Suppression of artifacts in phase-sensitive COSY. J. Magn. Reson. 100, 469–483.
Turner, C. J. and Hutton, W. C. (1993) A comparison of data-acquisition schemes in two-dimensional COSY experiments. J. Magn. Reson. Ser. A 105, 72–77.
Simorre, J.-P. and Marion, D. (1991) A method aimed at obtaining a complete set of cross peaks in single-scan high-resolution homonuclear 3D NMR J. Magn. Reson. 94, 426–432.
Glaser, S. and Kalbitzer, H. R. (1986) Improvement of two-dimensional NMR spectra by weighted mean t 1-ridge subtraction and antidiagonal reduction. J. Magn. Reson. 68, 350–354.
Manoleras, N. and Norton, R. S. (1992) Spectral processing methods for the removal of t 1 noise and solvent artifacts from NMR spectra. J. Biomol. NMR 2, 485–494.
Pelczer, I., Begemann, J., and Likos, J., unpublished.
Fortier, P. L., Delsuc, M. A., Guittet, E., Kahn, P., and Lallemand, J. Y. (1991) Convolution difference in the frequency domain and its use in 2D NMR. J. Magn. Reson. 95, 161–164.
Gibbs, A., Morris, G. A., Swanson, A. G., and Cowburn, D. (1993) Suppression of t 1 noise in 2D NMR spectroscopy by reference deconvolution. J. Magn. Reson. Ser. A 101, 351–356.
Boetgens, S., Meier, B. U., Griesinger, C., and Ernst, R. R. (1989) Local symmetry in 2D and 3D NMR spectra. J. Magn. Reson. 85, 337–358.
Griesinger, C., Gemperle, C., Sørensen, O. W., and Ernst, R. R. (1987) Symmetry in coherence transfer. Application to two-dimensional N.M.R. Mol. Phys. 62, 295–332.
Baumann, R., Kumar, A., Ernst, R. R., and Wüthrich, K. (1981) Improvement of 2D NOE and 2D correlated spectra by triangular multiplication. J. Magn. Reson. 44, 76–83.
Baumann, R., Wider, G., Ernst, R. R., and Wuthrich, K. (1981) Improvement of 2D NOE and 2D correlated spectra by symmetrization. J. Magn. Reson. 44, 402–406.
Mersh, J. D. and Sanders, J. K. M. (1982) Symmetrization of proton two-dimensional J spectra. J. Magn. Reson. 50, 171–174.
Neidig, K.-P. and Kalbitzer, H. R. (1991) Enhancement of global symmetries in two-dimensional NMR spectra. J. Magn. Reson. 91, 155–164.
Braunschweiler, L., Bodenhausen, G., and Ernst, R. R. (1983) Analysis of networks of coupled spins by multiple quantum N.M.R. Mol. Phys. 48, 535–560.
Bolton, P. H. (1986) Enhancement of two-dimensional spectra such as INADEQUATE by application of symmetry rules. J. Magn. Reson. 68, 180–184.
Lambert, J. and Buddrus, J. (1993) Sensitivity enhancement of two-dimensional 13C, 13C-INADEQUATE spectroscopy by considering symmetry and isotope shifts. J. Magn. Reson. Ser. A 101, 307–312.
Bax, A., Freeman, R., and Kempsell, S. P. (1980) Natural abundance 13C-13C coupling observed via double-quantum coherence. J. Am. Chem. Soc. 102, 4849–4851.
Bax, A. and Mareci, T. H. (1983) Practical aspects of carbon-13 double-quantum NMR. J. Magn. Reson. 53, 360–363.
Zuiderweg, E. R. P. (1986) COSY representation of two-dimensional homo-nuclear double-quantum spectra. J. Magn. Reson. 66, 153–156.
Grahn, H., Edlund, U., van den Hoogen, Y. Th., Altona, C., Delaglio, F., Roggenbuck, M. W., and Borer, P. N. (1989) Toward a computer assisted analysis of NOESY spectra: A multivariate data analysis of an RNA NOESY spectrum. J. Biomol. Struct. Dyn. 6, 1135–1150.
Hardy, J. K. and Rinaldi, P. L. (1990) Principal component analysis for artifact reduction in COSY spectra. J. Magn. Reson. 88, 320–333.
Brown, D. E. and Campbell, T. W. (1990) Enhancement of 2D NMR spectra using singular value decomposition. J. Magn. Reson. 89, 255–264.
Kupce, E. and Wrackmeyer, B. (1991) Local symmetrization in 1D NMR spectra. J. Magn. Reson. 91, 644–647.
Meier, B. U., Mádi, Z. L., and Ernst, R. R. (1987) Computer analysis of nuclear spin systems based on local symmetry in 2D spectra. J. Magn. Reson. 74, 565–573.
Shen, H., Ludvigsen, S., and Poulsen, F. M. (1990) Application of symmetry projection operators to measurements of coupling constants in 2D NMR spectra of proteins. J. Magn. Reson. 90, 346–354.
Oh, B. H., Westler, W. M., Darba, P., and Markley, J. L. (1988) Protein carbon-13 spin systems by a single two-dimensional nuclear magnetic resonance experiment. Science 240, 908–911.
Hoch, J. C., Hengyi, S., Kjaer, M., Ludvigsen, S., and Poulsen, F. M. (1987) Symmetry recognition applied two-dimensional NMR data. Carlsberg Res. Commun. 52, 111–122.
Kjaer, M. and Poulsen, F. M. (1991) Identification of 2D 1H NMR antiphase crosspeaks using a neural network. J. Magn. Reson. 94, 659–663.
Shen, H. and Poulsen, F. M. (1990) Toward automated determination of buildup rates of nuclear Overhauser effects in proteins, using symmetry operations. J. Magn. Reson. 89, 585–594.
Shen, H. and Poulsen, F. M. (1992) Group theoretical projection operators and symmetry-adapted fnnctions in NMR spectral analysts. J. Magn. Reson. 97, 385–390.
Mueller, L. (1987) P. E. COSY, a simple alternative to E. COSY. J. Magn. Reson. 72, 191–196.
Marion, D. and Bax, A. (1988) P. COSY, a sensitive alternative for double-quantum-filtered COSY. J. Magn. Reson. 80, 528–533.
Dalvit, C., Bovermann, G., and Widmer, H. (1990) Improved diagonal suppression in two-dimensional exchange experiments of molecules in the slow motion regime. J. Magn. Reson. 88, 432–439.
Davis, A. L., Keeler, J., Laue, E. D., and Moskau, D. (1992) Experiments for recording pure-absorption heteronuclear correlation spectra using pulsed field gradients. J. Magn. Reson. 98, 207–216.
Palmer A. G., III, Cavanagh, J., Wright, P. E., and Rance, M. (1991) Sensitivity improvement in proton-detected two-dimensional heteronuclear correlation NMR spectroscopy. J. Magn. Reson. 93, 151–170.
Palmer A. G., III, Cavanagh, J., Byrd, R. A., and Rance, M. (1992) Sensitivity improvement in three-dimensional heteronuclear correlation NMR spectroscopy. J. Magn. Reson. 96, 416–424.
Muhandiram, D. R., Xu, G. Y., and Kay, L. E. (1993) An enhanced-sensitivity pure absorption gradient 4D 15N, 13C-edited NOESY experiment. J. Biomol. NMR 3, 463–470.
Wang, K. Y., Heffron, G. J., Bishop. K. D., Levy, G. C., Garbesi, A. M., Tondelh, L., Medley, J. H., and Borer, P. N. (1992) Improved strategy for sequence-specific 13C NMR assignments in [d(CGTACGTACG)]2. Magn. Reson. Chem. 30, 377–380.
Robin, M., Delsuc, M.-A., Guittet, E., and Lallemand, J.-Y. (1991) Optimized acquisition and processing schemes in three-dimensional NMR spectroscopy. J. Magn. Reson. 92, 645–650.
Moy, F. J., Lowry, D. F., Matsumura, P., Dahlquist, F. W., Krywko, J. E., and Domaille, P. J. (1994) Assignments, secondary structure, global field, and dynamics of chemotaxis Y protein using three-and four-dimensional heteronuclear (13C, 15N) NMR spectroscopy. Biochemistry 33, 10,731–10,742.
Hodgkinson, P., Mott, H. R., Driscoll, P. C., Jones, J. A., and Hore, P. J. (1993) Application of maximum entropy methods to three-dimensional NMR spectroscopy. J. Magn. Reson. Ser. B 101, 218–222.
Jeong, G.-W., Borer, P. N., Wang, S. S., and Levy, G. C. (1993) Maximum-likelihood-constrained deconvolution of two-dimensional NMR spectra. Accuracy of spectral quantification. J. Magn. Reson. Ser. A 103, 123–134.
Mujeeb, A., Kerwin, S. M., Egan, W., Kenyon, G. L., and James, T. L. (1992) A potential gene target in HIV-1: Rationale, selection of a conserved sequence, and determination of NMR distance and torsion angle constraints. Biochemistry 31, 9325–9338.
Hoffman, R. E., Kumar, A., Bishop, K. D., Borer, P. N., and Levy, G. C. (1989) Application of the maximum likelihood method to a large 2D NMR spectrum using a parallel computer. J. Magn. Reson. 83, 586–594.
Donoho, D. L., Johnstone, I. M., Sterm A. S., and Hoch, J. C. (1990) Does the maximum entropy method improve sensitivity? Proc. Natl. Acad. Sci. USA 87, 5066–5068.
Carter, B. G., unpublished.
Zolnai, Zs, Westler, W. M., Ulrich, E. L., and Markley, J. L. (1990) Drafting table and light-box software for multidimensional NMR spectral analysis (PIXI). The personal computer workstation. J. Magn. Reson. 88, 511–522.
Olejniczak, E. T., Xu, R. X., Petros, A. M., and Fesik, S. W. (1992) Optimized constant-time 4D HNCAHA and HN(CO)CAHA experiments. Applications to the backbone assignments of the FKBP/ascomycin complex. J. Magn. Reson. 100, 444–450.
Cambell-Burk, S. L., Domaille, P. J., Starovasnik, M. A., Boucher, W., and Laue, E. D. (1992) Sequential assignment of the backbone nuclei (1H, 15N and 13C) of c-H-ras p21 (1–166). GDP using a novel 4D NMR strategy. J. Biomol. NMR 2, 639–646.
Lee, A. L., Kanaar, R., Rio, D. C., and Wemmer, D. E. (1994) Resonance assignments and solution structure of the second RNA-binding domain of sex-lethal determined by multidimensional heteronuclear magnetic resonance. Biochemistry 33, 13,775–13,786.
Rouh, A., Louis-Joseph, A., and Lallemand, J.-Y (1994) Bayesian signal extraction from noisy FT NMR spectra. J. Biomol. NMR 4, 505–518.
Wagner, G. (1984) Two-dimensional relayed coherence transfer-NOE spectroscopy. J. Magn. Reson. 57, 497–505.
Pelczer, I., Xu, J., Neirinck, P., and Szafranski, M. S. (1993) COSYDD, An alternative look at low resolution correlation spectra (COSY) with advantage for automated assignment. Poster at 1993 Eastern Analytical Symposium, Somerset, NJ, Nov 14–19, #355.
Neirinck, P. and Pelczer, I. (1994) Lineshape, resolution and coupling constants further considerations for COSYDD. Poster at 35th ENC, April 10–15, Pacific Grove, CA (MP 124).
Turner, D. L. (1993) Optimization of COSY and related methods. Application to 1H NMR of horse ferricytohrome c. J. Magn. Reson. Ser. A 104, 197–202.
Biamonti, C., Rios, C., Lyons, B. A., and Montelione, G. T. (1994) Multidimensional NMR experiments and analysis techniques for determining homo-and heteronuclear scalar coupling constants in proteins and nucleic acids. Adv. Biophys. Chem. 4, 51–120.
Bax, A., Vuister, G. W., Grzesiek, S., Delaglio, F., Wang, A. C., Tschudin, R., and Zhu, G. (1994) Measurement of homo-and heteronuclear J couplings from quantitative J correlations. Meth. Enzymol. 239, 79–105.
Freeman, R. and McIntyre, L. (1992) Fine structure in NMR correlation spectroscopy. Israel J. Chem. 32, 231–244.
Griesinger, C., Schwalbe, H., Schleucher, J., and Sattler, M. (1994) Proton-detected heteronuclear and multidimensional NMR. Chapter 3. in Ref (30), p. 458–580.
Neuhaus, D., Wagner, G., Vasak, M., Kagi, J. H. R., and Wuthrich, K. (1985) Systematic application of high-resolution, phase-sensitive two-dimensional 1H-NMR techniques for the identification of the amino-acid-proton spin systems in proteins. Eur. J. Biochem. 151, 257–273.
Bax, A. and Lerner, L. (1988) Measurement of 1H-1H coupling constants in DNA fragments by 2D NMR. J. Magn. Reson. 79, 429–438.
Kay, L. E. and Bax, A. (1990) New methods for the measurement of NH-CH coupling constants in 15N-labeled proteins. J. Magn. Reson. 86, 110–126.
Delaglio, F., Torchia, D. A., and Bax, A. (1991) Measurement of 15N-13C J couplings in staphylococcal nuclease. J. Biomol. NMR 1, 439–446.
Vuister, G. W., Delaglio, F., and Bax, A. (1993) The use of 1JCH coupling constants as a probe for protein backbone conformation. J. Biomol. NMR 3, 67–80.
Kay, L. E., Brooks, B., Sparks, S. W., Torchia, D. A., and Bax, A. (1989) Measurement of NH-CH coupling constants in staphylococcal nuclease by two-dimensional NMR and comparison with X-ray crystallographic results. J. Am. Chem. Soc. 111, 5488–5490.
Norwood, T. J., Crawfors, D. A., Steventon, M. E., Driscoll, P. C., and Campbell, I. D. (1992) Heteronuclear 1H-15N nuclear magnetic resonance studies of the c subunit of the Escherichia coli F1F0 ATP synthase: Assignment and secondary structure. Biochemistry 31, 6285–6290.
Oschkinat, H. and Freeman, R. (1984) Fine structure in two-dimensional NMR correlation spectroscopy. J. Magn. Reson. 60, 164–169.
Kessler, H. and Oschkinat, H. (1985) Simplification of spectra for the determination of coupling constants from homonuclear correlated 2D NMR spectra. Angew. Chem. Int. Ed. Engl. 24, 690–692.
Kessler, H., Muller, A., and Oschkinat, H. (1985) Differences and sums of traces within COSY spectra (DISCO) for the extraction of coupling constants. ‘Decoupling’ after the measurement. Magn. Reson. Chem. 23, 844–852.
Griesinger, C., Sørensen, O. W., and Ernst, R. R. (1985) Two-dimensional correlation of connected NMR transitions. J. Am. Chem. Soc. 107, 6394–6396.
Griesinger, C., Sørensen, O. W., and Ernst, R. R. (1986) Correlation of connected transitions by two-dimensional NMR spectroscopy. J. Magn. Reson. 85, 6837–6852.
Griesinger, C., Sarensen, O. W., and Ernst, R. R. (1987) Practical aspects of the E.COSY technique. Measurement of scalar spin-spin coupling constants in peptides. J. Magn. Reson. 75, 474–492.
Sørensen, M. D., Led, J. J., and Sørensen, O. W. (1994) A new 2D NMR method for measurement of JHH coupling constants. J. Biomol. NMR 4, 135–141.
Bauer, W. and Griesinger, C. (1993) Vinyllithium: dynamic behavior in tetrahydrofurane solution and comprehensive analysts of NMR spin-spin coupling constants. J. Am. Chem. Soc. 115, 10,871–10,882.
Vuister, G. W. and Bax, A. (1994) Measurement of four-bond HN-H J-couplings in staphylococcal nuclease. J. Biomol. NMR 4, 193–200.
Neri, D., Otting, G., and Wuthrich, K. (1990) New nuclear magnetic resonance experiment for measurements of the vicinal coupling constants 3 J HN in proteins. J. Am. Chem. Soc. 112, 3663–3665.
Billeter, M., Neri, D., Otting, G., Qian, Y. Q., and Wuthrich, K. (1992) Precise vicinal coupling constants 3 J HN in proteins from nonlinear fits of J-modulated [15N, 1H]-COSY experiments. J. Biomol. NMR 2, 257–274.
Fogolari, F., Esposito, G., Cauci, S., and Viglino, P. (1993) Evaluation of J coupling constants from peak amplitudes of total correlation spectra. J. Magn. Reson., Ser. A 102, 49–57.
Blake, P. R., Lee, B., Summers, M. F., Adams, M. W. W., Park, J.-B., Zhou, Z. H., and Bax, A. (1992) Quantitative measurement of small through-hydrogen-bond and ‘through-space’ 1H-113Cd and 1H-199Hg J couplings in metal-substituted rubredoxin from Pyrococcus furiosus. J. Biomol. NMR 2, 527–533.
van Duynhoven, J. P. M., Goudriann, J., Hilbers, C. W., and Wijmenga, S. S. (1992) Quantitative evaluation of TOCSY data. Application to sugar ring conformational analysis. J. Am. Chem. Soc. 114, 10,055–10,056.
Vuister, G. W. and Bax, A. (1993) Measurement of two-and three-bond proton to methyl-carbon J couplings in proteins uniformly enriched with 13C. J. Magn. Reson., Ser. B 102, 228–231.
Pelczer, I. and Szafranski, M. S. (1994) J-Coupling constants from homonuclear correlations. Lecture at Advanced School on NMR in Biology and Medicine: “NMR inside biology: from models to in vivo,” Altavilla Militia (Palermo), Italy, Sept. 21–30.
Szafranski, M. S. and Pelczer, I. (1994) A novel approach for extracting homonuclear coupling constants from the evolution of MQ coherences combining information from the time and frequency domain. Poster at 35th ENC, April 10–15, Pacific Grove, CA (MP 109).
Kim, Y. and Prestegard, J. H. (1989) Measurement of vicinal couplings from crosspeaks in COSY spectra. J. Magn. Reson. 84, 9–13.
Szyperski, T., Güntert, P., Otting, G., and Wüthrich, K. (1992) Determination of scalar coupling constants by inverse Fourier transformation of in-phase multiplets. J. Magn. Reson. 99, 552–560.
Wuthrich, K., personal communication.
Schwalbe, H., Marino, J. P., King, G. C., Wechselberger, R., Bermel, W., and Griesinger, C. (1994) Determination of a complete set of coupling constants in 13C-labeled oligonucleotides. J. Biomol. NMR 4, 631–644.
Ludvigsen, S., Andersen, K. V., and Paulsen, F. M. (1991) Accurate measurements of coupling constants from two-dimensional nuclear magnetic resonance spectra of proteins and determination of φ-angles. J. Mol. Biol. 217, 731–736.
Widmer, H. and Wüthrich, K. (1987) Simulated two-dimensional NMR crosspeak fine structures for 1H spin systems in polypeptides and polydeoxynucleotides. J. Magn. Reson. 74, 316–336.
Majumdar, A., and Hosur, R. V. (1992) Simulation of 2D NMR spectra for determination of solution conformations of nucleic acids. Prog. NMR Spectrosc. 24, 109–158.
Hosur, R. V., Majumdar, A., Mukhopadhyay, N., and Govil, G. (1991) Sequence effects in the solution structure of DNA:NMR approach. Ind J. Chem. 30B, 97–106.
Smith, L. J., Sutcliffe, M. J., Redfield, C., and Dobson, C. M. (1991) Analysis of and χ1 torsion angles for hen lysozyme in solution from 1H NMR spin-spin coupling constants. Biochemistry 30, 986–996.
Bartik, K. and Redfield, C. (1993) A method for the estimation of κ torsion angles in proteins. J. Biomol. NMR 3, 415–428.
Macaya, R. F., Schultze, P., and Feigon, J. (1992) Sugar conformations in intramolecular DNA triplexes determined by coupling constants obtained by automated simulation of P. COSY crosspeaks. J. Am. Chem. Soc. 114, 781–783.
Widmer, H. and Wüthrich, K. (1986) Simulation of two-dimensional NMR experiments using numerical density matrix calculations. J. Magn. Reson. 70, 270–279.
Celda, B., Widmer, H., Leupin, W., Chazm, W. J., Denny, W. A., and Wuthrich, K. (1989) Conformational studies of d-(AAAAATTTTT)2 using constraints from nuclear Overhauser effects and from quantitative analysis of the cross-peak fine structures in two-dimensional 1H nuclear magnetic resonance spectra. Biochemistry 28, 1462–1471.
Gochin, M., Zon, G., and James, T. L. (1990) Two-dimensional COSY and two-dimensional NOE spectroscopy of d(AC)4 · d(GT)4: Extraction of structural constraints. Biochemistry 29, 11,16l–11,171.
Stolarski, R., Egan, W., and James, T. L. (1992) Solution structure of the EcoRI DNA octamer containing 5-fluorouracil via restrained molecular dynamics using distance and torsion angle constraints extracted from NMR spectral simulations. Biochemistry 31, 7027–7042.
Weisz, K., Shafer, R. H., Egan, W., and James, T. L. (1992) The octamer motif in immunoglobulin genes: Extraction of structural constraints from two-dimensional NMR studies. Biochemistry 31, 7477–7487.
Titman, J. J. and Keeler, J. (1990) Measurement of homonuclear coupling constants from NMR correlation spectra. J. Magn. Reson. 89, 640–646.
Schwalbe, H., Samstag, W., Engels, J. W., Bermel, W., and Griesinger, C. (1993) Determination of 3J(C,P) and 3J(H,P) coupling constants in nucleotide oligomers with FIDS-HSQC. J. Biomol. NMR 3, 479–486.
Huber, P. and Bodenhausen, G. (1993) Simplification of multiplets by deconvolution in one-and two-dimensional NMR spectra. J. Magn. Reson., Ser. A 102, 81–89.
Delsuc, M. A. and Levy, G. C. (1988) The application of maximum entropy processing to the deconvolution of coupling patterns in NMR. J. Magn. Reson. 76, 306–315.
Weiss, G. H., Kiefer, J. E., and Ferretti, J. A. (1992) Accuracy and precision in the estimation of internuclear distances for structure determination. J. Magn. Reson. 97, 227–234.
Bonvin, A. M. J. J. (1993) Determination of biomolecular structures by NMR. Use of relaxation matrix calculations. Ph.D. Thesis, Utrecht University, Utrecht, The Netherlands.
Davis, A. L., Estcourt, G., Keeler, J., Laue, E. D., and Titman, J. J. (1993) Improvement of z filters and purging pulses by the use of zero-quantum dephasing in inhomogeneous B1 or B0 fields. J. Magn. Reson., Ser. A 105, 167–183.
Wang, K.-Y., Borer, P. N., Levy, G. C., and Pelczer, I. (1992) Evaluation of zero-quantum effects on quantitative analysts of NOE intensities. J. Magn. Reson. 96, 165–170.
Hore, P. J., Grainger, D. S., Wimperis, S., and Daniell, G. J. (1990) Suppression of J crosspeaks in NOESY spectra by the maximum entropy method. J. Magn. Reson. 89, 415–422.
Wang, H., Glick, G. D., and Zutderweg, E. R. P. (1993) A three-dimensional method for the separation of zero-quantum coherence and NOE in NOESY spectra. J. Magn. Reson., Ser. A 102, 116–121.
Kleywegt, G. J., Vuister, G. W., Padilla, A., Knegtel, R. M. A., Boelens, R., and Kaptein, R. (1993) Computer-assisted assignment of homonuclear 3D NMR spectra of proteins. Application to pike parvalbumin III. J. Magn. Reson., Ser. B 102, 166–176.
Grzestek, S., Dobeli, H., Gentz, R., Garotta, G., Labhardt, A. M., and Bax, A. (1992) 1H, 13C, and 15N NMR Backbone assignments and secondary structure of human interferon-γ. Biochemistry 31, 8180–8190.
Logan, T. M., Olejniczak, E. T., Xu, R. X., and Fesik, S. W. (1993) A general method for assigning NMR spectra of denaturated proteins using 3D HC(CO)NH-TOCSY triple resonance experiments. J. Biomol. NMR 3, 225–231.
Bernstein, R., Cieslar, C., Ross, A., Oschkinat, H., Freund, J., and Holak, T. A. (1993) Computer-assisted assignment of multidimensional NMR spectra of proteins. Application to 3D NOESY-HMQC and TOCSY-HMQC spectra. J. Biomol. NMR 3, 245–251.
Hare, B. J. and Prestegard, J. H. (1994) Application of neural networks to automated assignment of NMR spectra of proteins. J. Biomol. NMR 4, 35–46.
van de Ven, F. J. (1990) PROSPECT, A program for automated interpretation of 2D NMR spectra of proteins. J. Magn. Reson. 86, 633–644.
Zimmerman, D., Kulikowski, C., Wang, L., Lyons, B., and Montelione, G. T. (1994) Automated sequencing of amino acid spin systems in proteins using multidimensional HCC(CO)NH-TOCSY spectroscopy and constraint propagation methods from artificial intelligence. J. Biomol. NMR 4, 241–256.
Olson, J. B., Jr. and Markley, J. L. (1994) Evaluation of an algorithm for the automated sequential assignment of protein backbone resonances. A demonstration of the connectivity tracing assignment tools (CONTRAST) software package. J. Biomol. NMR 4, 385–410.
Meadows, R. P., Olejniczak, E. T., and Fesik, S. W. (1994) A computer-based protocol for semiautomated assignments and 3D structure determination of proteins. J. Biomol. NMR 4, 79–96.
Jun, Xu, J. and Borer, P. N. (1994) Rigorous deduction theory for assignment of multidimensional NMR spectra using the independent spur coupling network approach. J. Chem. Inf. Comp. Sci. 34, 349–356.
Jun, Xu, J., Weber, P., and Borer, P. N. (1995) Computer assisted assignment of peptides with non-standard amino acids. J. Biomol. NMR, accepted.
Szalma, S. and Kalnik, M. W. (1994) Computer assisted assignment of proteins. Poster #WP-97 at 35th ENC, April 10–15, Pacific Grove, CA, abstr.: p. 257.
Oschkinat, H. and Croft, D. (1994) Automated assignment of multidimensional nuclear magnetic resonance spectra. Meth. Enzymol. 239, 308–318.
Levy, G. C., Delaglio, F., Macur, A., and Begemann, J. (1986) NMR2: A powerful software system for processing multi-dimensional NMR data. Comp. Enh. Spectrosc. 3, 1–12.
The latest version of the GIFA software package is also available through anonymous FTP from http://tome.cbs.univ-montpl.fr. (M. A. Delsuc, personal communication).
Spitzfaden, C., Braun, W., Wider, G., Widmer, H., and Wüthrich, K. (1994) Determination of the NMR solution structure of the cyclophilin A-cyclosporin A complex. J. Biomol. NMR 4, 463–482.
Burgering, M., Boelens, R., and Kaptein, R. (1993) Observation of intersubunit NOEs in a dimeric P22 Mnt repressor mutant by a time-shared [15N, 13C] double half-filter technique. J. Biomol. NMR 3, 709–714.
Katahira, M., Knegtel, R. M. A., Boelens, R., Eib, D., Schilthuis, J. G., van der Saag, P. T., and Kaptein, R. (1992) Homo-and heteronuclear NMR studies of the human retionoic acid receptor DNA-binding domain: Sequential assignments and identification of secondary structural elements. Biochemistry 31, 6474–6480.
Osterhout, J. J., Jr, Handel, T., Na, G., Toumadje, A., Long, R. C., Connolly, P. J., Hoch, J. C., Johnson, W. C., Jr., Live, D., and DeGrado, W. F. (1992) Characterization of the structural properties of α1B, a peptide designed to form a four-helix bundle. Biochemistry 114, 331–337.
Ludvigsen, S., Roy, M., Thøgersen, H., and Kaarsholm, N. C. (1994) High-resolution structure of an engineered biologically potent insulin monomer, B16 Tyr-His, as determined by nuclear magnetic resonance spectroscopy. Biochemistry 33, 7998–8006.
Andersen, K. V. and Poulsen, F. M. (1993) The three-dimensional structure of acyl-coenzyme A binding protein from bovine liver: Structural refinement using heteronuclear multidimensional NMR spectroscopy. J. Biomol. NMR 3, 271–284.
SPARKY is available by contacting Prof. T. L. James (UCSF) (T. L. James, personal communication).
Cieslar, C., Ross, A., Zink, T., and Holak, T. A. (1993) Efficiency in multidimensional NMR by optimized recording of time domain point-phase pans in evolution periods and their selective linear transformation. J. Magn. Reson., Ser. B 101, 97–101.
Zink, T., Ross, A., Luers, K., Cieslar, C., Rudolph, R., and Holak, T. A. (1994) Structure and dynamics of the human granulocyte colony-stimulating factor determined by NMR spectroscopy. Loop mobility in a four-helix-bundle peptide. Biochemistry 33, 8453–8463.
Zhou, M.-M, Logan, T. M., Thériault, Y., Van Etten, R. L., and Fesik, S. W. (1994) Backbone 1H, 13C, and 15N assignments and secondary structure of bovine low molecular weight phosphotyrosyl protein phosphatase. Biochemistry 33, 5221–5229.
Hansen, A. P., Petros, A. M., Meadows, R. P., Nettesheim, D. G., Mazar, A. P., Olejniczak, E. T., Xu, R. X., Pederson, T. M., Henkin, J., and Fesik, S. W. (1994) Solution structure of the amino-terminal fragment of urinokinase-type plasminogen activator. Biochemistry 44, 4847–4864.
NMRView is available electronically from Dr. Bruce Johnson (bruce_johnson@merck.com).
ANSIG is now available from Dr. Per Kraulis on request (kraulis@sto.pharmacia.se).
Griesinger, C., Sørensen, O. W., and Ernst, R. R. (1987) Novel three-dimensional NMR techniques for studies of peptides and biological macromolecules. J. Am. Chem. Soc. 109, 7227–7228.
Simorre, J.-P., Caille, A., Marion, D., Marion, D., and Ptak, M. (1991) Two-and three-dimensional 1H NMR studies of a wheat phospholipid transfer protein. Sequential resonance assignments and secondary structure. Biochemistry 30, 11,600–11,608.
Archer, S. J., Bax, A., Roberts, A. B., Sporn, M. B., Ogawa, Y., Piez, K. A., Weatherbee, J. A., Tsang, M. L.-S., Lucas, R., Zheng, B.-L., Wenker, J., and Torchia, D. A. (1993) Transforming growth factor β1: Secondary structure as determined by heteronuclear magnetic resonance spectroscopy. Biochemistry 32, 1164–1171.
Ames, J. B., Tanaka, T., Stryer, L., and Ikura, M. (1994) Secondary structure of myristoylated recoverin determined by three-dimensional heteronuclear NMR. Implications for the calcium-myristoyl switch. Biochemistry 33, 10,743–10,753.
Forman-Kay, J. D., Clore, G. M., Stahl, S. J., and Gomenborn, A. M. (1992) 1H and 15N resonance assignments and secondary structure of the human thioredoxin C62A, C69A, C73A mutant. J. Biomol. NMR 2, 431–445.
Van Doren, S. R., Kurochkin, A. V., Ye, Q.-Z., Johnson, L. L., Hupe, D. J., and Zuiderweg, E. R. P. (1993) Assignments for the main-chain nuclear magnetic resonances and delineation of the secondary structure of the catalytic domain of human stromelysin-1 as obtained from triple-resonance 3D NMR experiments. Biochemistry 32, 13,109–13,122.
Remerowski, M. L., Domke, T., Gronewegen, A., Pepermans, H. A. M., Hilbers, C. W., and van de Ven, F. J. M. (1994) 1H, 13C and 15N NMR backbone assignments and secondary structure of the 269-residue protease subtilism 309 from Bacillus lentus. J. Biomol. NMR 4, 257–278.
Garrett, D. S., Lodi, P. J., Shamoo, Y., Williams, K. R., Clore, G. M., and Gronenborn, A. M. (1994) Determination of the secondary structure and folding topology of an RNA binding domain of mammalian hnRNP A1 protein using three-dimensional heteronuclear magnetic resonance spectroscopy. Biochemistry 33, 2852–2858.
van Tongeren, B. P. O., Mehlkopf, A. F., van Ormondt, D., Schramp, M., and de Beer, R. (1992) Embedding a PRO-MATLAB into NMR signal-processing applications, based on C++ and the X-window system. J. Magn. Reson. 100, 619–624.
Wolfram, S. (1988) Mathematica. A system for Doing Mathematics by Computer. Addison-Wesley, Redwood City, CA.
Guntert, P., Schaefer, N., Otting, G., and Wuthrich, K. (1993) POMA: A complete Mathematica implementation of the NMR product-operator formalism. J. Magn. Reson., Ser. A 101, 103–105.
Szafranski, M. S. and Pelczer, I., unpublished.
Böcskei, Zs, Groom, C. R., Flower, D. R., Wright, C. E., Phillips, S. E. V., Cavaggioni, A., Findlay, J. B. C., and North, A. C. T. (1992) Pheromone binding to two urinary proteins revealed by X-ray crystallography. Nature 360, 186–188.
Redfield, C. and Dobson, C. M. (1988) Sequential 1H NMR assignments and secondary structure of hen egg white lysozyme in solution. Biochemistry 27, 122–136.
Wang, A. C., Lodi, P. J., Qin, J., Vuister, G. W., Gronenborn, A. M., and Clore, G. M. (1994) An efficient triple-resonance experiment for proton-detected sequential backbone assignment of medium-sized proteins. J. Magn. Reson., Ser. B 105, 196–198.
PRONTO/3D is now available through anonymous FTP (Kjaer, M., personal communication).
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Pelczer, I., Carter, B.G. (1997). Data Processing in Multidimensional NMR. In: Reid, D.G. (eds) Protein NMR Techniques. Methods in Molecular Biology™, vol 60. Humana Press. https://doi.org/10.1385/0-89603-309-0:71
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