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References
Atreya HS, Szyperski T (2004) G-matrix Fourier transform NMR spectroscopy for complete protein resonance assignment. Proc Natl Acad Sci USA 101:9642–9647
Bodenhausen G, Ernst RR (1981) The accordion experiment, a simple approach to 3-dimensional NMR-spectroscopy. J Magn Reson 45:367–373
Brutscher B, Cordier F, Simorre JP, Caffrey MS, Marion D (1995a) High-resolution 3D HNCOCA experiment applied to a 28-kDa paramagnetic protein. J Biomol NMR 5:202–206
Brutscher B, Morelle N, Cordier F, Marion D (1995b) Determination of an initial set of NOE-derived distance contraints for the structure determination of N-15/C-13-labeled proteins. J Magn Reson B109:238–242
Cavanagh C, Fairbrother WJ, Palmer AG, Skelton NJ (1996) Protein NMR spectroscopy. Academic, San Diego
Coggins BE, Venters RA, Zhou P (2003) Generalized reconstruction of n-D NMR spectra from multiple projections: application to the 5-D HACACONH spectrum of protein G B1 domain. J Am Chem Soc 126:1000–1001
Constans A (2003) NMR hits the big time. Scientist 17:45–48
Ding K, Gronenborn AM (2002) Novel 2D triple-resonance NMR experiments for sequential resonance assignments of proteins. J Magn Reson 156:262–268
Ding K, Gronenborn AM (2003) Simultaneous and accurate determination of one-bond 15N--13C′ and two-bond 1HN-13C′ dipolar couplings. J Am Chem Soc 125:11504–1150
Ernst RR, Bodenhausen G, Wokaun A (1987) Principles of nuclear magnetic resonance in one and two dimensions. Oxford University Press, London
Gardner K, Kay LE (1998) The use of 2H, 13C, 15N multidimensional NMR to study the structure and dynamics of proteins. Annu Rev Biophys Biomol Struct 27:357–406
Grage H, Akke M (2003) A statistical analysis of NMR spectrometer noise. J Magn Reson 162:176–188
Hoch JC, Stern AS (1996) NMR data processing. Wiley-Liss, New York
Hoshino M, Otting G (2004) Sensitivity-enhanced double-TROSY experiment for simultaneous measurement of one-bond (15)N-(1)H, (15)N-(13)C′ and two-bond (1)H-(13)C′ couplings. J Magn Reson 171:270–276
Kay LE, Prestegard JH (1988) Spin-lattice relaxation of coupled spins from 2D Accordion spectroscopy. J Magn Reson 77:599–605
Kim S, Szyperski T (2003) GFT NMR, a new approach to rapidly obtain precise high-dimensional spectral information. J Am Chem Soc 125:1385–1393
Kim S, Szyperski T (2004) GFT NMR experiment for polypeptide backbone and 13Cβ chemical shift assignment. J Biomol NMR 28:117–130
Kontaxis G, Keeler J (1995) The accordion approach for „Taylored“ TOCSY. J Magn Reson 115:35–4
Kupče E, Freeman R (2003) Projection-reconstruction of three-dimensional NMR spectra. J Am Chem Soc 125:13958–13959
Kupče E, Freeman R (2004) Fast reconstruction of four-dimensional NMR spectra from plane projections. J Biomol NMR 28:391–395
Liu G, Shen Y, Atreya HS, Parish D, Shao Y, Sukumaran D, Xiao R, Yee A, Lemak A, Bhattacharya A, Acton TA, Arrowsmith CH, Montelione GT, Szyperski T (2005) NMR data collection and analysis protocol for high-throughput protein structure determination. Proc Natl Acad Sci USA 102:10487–10492
Löhr F, Rüterjans H (1995) A new experiment for the sequential assignment of backbone resonances in proteins. J Biomol NMR 6:189–197
Mandel AM, Palmer AG (1994) Measurement of relaxation-rate constants using constant-time accordion NMR spectroscopy. J Magn Reson 110:62–72
Marion D, Wüthrich K (1983) Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling-constants in proteins. Biochem Biophys Res Commun 113:967–974
Montelione GT, Zheng D, Huang Y, Gunsalus C, Szyperski T (2000) Protein NMR spectroscopy for structural genomics. Nat Struct Biol 7:982–984
Moseley HNB, Monleon D, Montelione GT (2001) Automatic determination of protein backbone resonance assignments from triple resonance nuclear magnetic resonance data. Methods Enzymol 339:91–108
Moseley HNB, Riaz N, Aramini JM, Szyperski T, Montelione GT (2004) A generalized approach to automated NMR peak list editing: application to reduced dimensionality triple resonance spectra. J Magn Reson 170:263–277
Pervushin K, Riek R, Wider G, Wüthrich K (1997) Attenuated T-2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution. Proc Natl Acad Sci USA 94:12366–12371
Pervushin K, Vogeli B, Eletsky A (2002) Longitudinal 1H relaxation optimization in TROSY NMR spectroscopy. J Am Chem Soc 124:12898–12902
Prestegard JH (1998) New techniques in structural NMR-anisotropic interactions. Nat Struct Biol 5:517–522
Service RF (2003) Propelled by recent advances, NMR moves into the fast lane. Science 299:503
Szyperski T, Wider G, Bushweller JH, Wüthrich K (1993a) 3D 13C-15N heteronuclear two-spin coherence spectroscopy for polypeptide backbone assignments in 13C-15N-double labeled proteins. J Biomol NMR 3:127–132
Szyperski T, Wider G, Bushweller JH, Wüthrich K (1993b) Reduced dimensionality in triple resonance NMR experiments. J Am Chem Soc 115:9307–9308
Szyperski T, Pellecchia M, Wüthrich K (1994) 3D Hα/βCα/β(CO)NHN, a Projected 4D NMR experiment for the sequential correlation of polypeptide 1Hα/β, 13Cα/β and backbone 15N and 1HN chemical shifts. J Magn Reson B105:188–191
Szyperski T, Braun D, Fernandez C, Bartels C, Wüthrich K (1995) A novel reduced-dimensionality triple resonance experiment for efficient polypeptide backbone assignment, 3D COHNNCA. J Magn Reson B 108:197–203
Szyperski T, Braun D, Banecki B, Wüthrich K (1996) Useful information from axial peak magnetization in projected NMR experiments. J Am Chem Soc 118:8147–8148
Szyperski T, Banecki B, Braun D, Glaser RW (1998) Sequential assignment of medium-sized 15N/13C-labeled proteins with projected 4D triple resonance NMR experiments. J Biomol NMR 11:387–405
Szyperski T, Yeh DC, Sukumaran DK, Moseley HNB, Montelione GT (2002) Reduced-dimensionality NMR spectroscopy for high-throughput protein resonance assignment. Proc Natl Acad Sci USA 99:8009–8014
Tjandra N, Bax A (1997) Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium. Science 278:1111–1114
Tolman JR, Prestegard JH (1996) Measurement of amide 15N-1H one-bond couplings in proteins using accordion heteronuclear shift correlation experiments. J Magn Reson B 112:269–274
Xia Y, Arrowsmith C, Szyperski T (2002) Novel projected 4D triple resonance experiments for polypeptide chemical shift assignment. J Biomol NMR 24:41–51
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Szyperski, T. (2006). Principles and Application of Projected Multidimensional NMR Spectroscopy — G-matrix Fourier Transform NMR. In: Arrondo, J.L.R., Alonso, A. (eds) Advanced Techniques in Biophysics. Springer Series in Biophysics, vol 10. Springer, Berlin, Heidelberg . https://doi.org/10.1007/3-540-30786-9_7
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