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Solution NMR spectroscopy beyond 25 kDa
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Kay LE, Gardner KH. Solution NMR spectroscopy beyond 25 kDa. Curr Opin Struct Biol. 7:1997;722-731.
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Curr Opin Struct Biol
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Kay, L.E.1
Gardner, K.H.2
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2
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0030612833
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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
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1H multiplet decreases with increasing field strength and that broad multiplet components can be eliminated with the phase cycling of the TROSY experiment. In perdeuterated proteins at an optimal field strength of around 1 GHz, the line width of the sharp component is expected to be nearly independent of the molecular size.
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1H multiplet decreases with increasing field strength and that broad multiplet components can be eliminated with the phase cycling of the TROSY experiment. In perdeuterated proteins at an optimal field strength of around 1 GHz, the line width of the sharp component is expected to be nearly independent of the molecular size.
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Proc Natl Acad Sci USA
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Pervushin, K.1
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3
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0031000510
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Direct measurement of angles between bond vectors in high-resolution NMR
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of special interest. It is shown that the angle between two bond vectors, N-H and C-H, can be obtained from the difference between the relaxation rates of multiplet components of the N-C multiple quantum coherence.
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Reif B, Hennig M, Griesinger C. Direct measurement of angles between bond vectors in high-resolution NMR. of special interest Science. 276:1997;1230-1233 It is shown that the angle between two bond vectors, N-H and C-H, can be obtained from the difference between the relaxation rates of multiplet components of the N-C multiple quantum coherence.
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Science
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Reif, B.1
Hennig, M.2
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13C' (carbonyl) chemical shift anisotropy mechanisms
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13C' (carbonyl) chemical shift anisotropy mechanisms. J Am Chem Soc. 119:1997;11938-11940.
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J Am Chem Soc
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Yang, D.1
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Kay, L.E.3
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6
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0029050883
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Nuclear magnetic dipole interactions in field-oriented proteins: Information for structure determination in solution
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Tolman JR, Flanagan JM, Kennedy MA, Prestegard JH. Nuclear magnetic dipole interactions in field-oriented proteins: information for structure determination in solution. Proc Natl Acad Sci USA. 92:1995;9279-9283.
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Tolman, J.R.1
Flanagan, J.M.2
Kennedy, M.A.3
Prestegard, J.H.4
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8
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0030018695
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15N enriched human ubiquitin resulting from relaxation interference and residual dipolar coupling
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15N enriched human ubiquitin resulting from relaxation interference and residual dipolar coupling. J Am Chem Soc. 118:1996;6264-6272.
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Tjandra, N.1
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Bax, A.3
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10
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1H one-bond couplings in proteins using accordion heteronuclear-shift-correlation experiments
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1H one-bond couplings in proteins using accordion heteronuclear-shift-correlation experiments. J Magn Reson. 112:1996;269-274.
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Tolman, J.R.1
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11
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0031063544
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CH splittings from magnetic-field dependence of J modulation in two-dimensional NMR spectra
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CH splittings from magnetic-field dependence of J modulation in two-dimensional NMR spectra. J Magn Reson. 124:1997;512-515.
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J Magn Reson
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Tjandra, N.1
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0032042263
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Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra
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Ottiger M, Delaglio F, Bax A. Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra. J Magn Reson. 131:1998;373-378.
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Ottiger, M.1
Delaglio, F.2
Bax, A.3
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13
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0030722243
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Direct measurement of distances and angles in biomolecules by NMR in dilute liquid crystalline medium
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of outstanding interest. Large residual dipolar couplings can be measured if proteins are dissolved in a solvent containing magnetically oriented bicelles in a liquid-crystalline phase. This technique makes the measurement of residual dipolar couplings possible, even for smaller proteins without a paramagnetic center, and improves the quality of NMR structures by adding additional constraints.
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Tjandra N, Bax A. Direct measurement of distances and angles in biomolecules by NMR in dilute liquid crystalline medium. of outstanding interest Science. 278:1997;1111-1114 Large residual dipolar couplings can be measured if proteins are dissolved in a solvent containing magnetically oriented bicelles in a liquid-crystalline phase. This technique makes the measurement of residual dipolar couplings possible, even for smaller proteins without a paramagnetic center, and improves the quality of NMR structures by adding additional constraints.
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Science
, vol.278
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Tjandra, N.1
Bax, A.2
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14
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0031244139
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High-resolution heteronuclear NMR of human ubiquitin in an aqueous liquid crystalline medium
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of special interest. The dilute bicelles have no effect on the transverse relaxation rates. The protein alignment is proportional to the bicelle concentration, which makes the size of the residual dipolar coupling become a tunable parameter.
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Bax A, Tjandra N. High-resolution heteronuclear NMR of human ubiquitin in an aqueous liquid crystalline medium. of special interest J Biomol NMR. 10:1997;289-292 The dilute bicelles have no effect on the transverse relaxation rates. The protein alignment is proportional to the bicelle concentration, which makes the size of the residual dipolar coupling become a tunable parameter.
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(1997)
J Biomol NMR
, vol.10
, pp. 289-292
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Bax, A.1
Tjandra, N.2
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15
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0024295725
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Magnetic field induced ordering of bile salt/phospholipid micelles: New media for NMR structural investigations
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Ram P, Prestegard JH. Magnetic field induced ordering of bile salt/phospholipid micelles: new media for NMR structural investigations. Biochim Biophys Acta. 940:1988;289-294.
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Ram, P.1
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0026774489
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Characterization of magnetically orientable bilayers in mixtures of dihexanoylphosphatidylcholine and dimyristoylphosphatidylcholine by solid-state NMR
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Sanders CR II, Schwonek JP. Characterization of magnetically orientable bilayers in mixtures of dihexanoylphosphatidylcholine and dimyristoylphosphatidylcholine by solid-state NMR. Biochemistry. 31:1992;8898-8905.
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Sanders C.R. II1
Schwonek, J.P.2
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33747570634
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Magnetically oriented phospholipid bilayered micelles for structural studies of polypeptides: Does the ideal bicelle exist?
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Vold RR, Prosser RS. Magnetically oriented phospholipid bilayered micelles for structural studies of polypeptides: does the ideal bicelle exist? J Magn Reson. 113:1996;267-271.
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Vold, R.R.1
Prosser, R.S.2
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19
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0031969085
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Magnetically aligned phospholipid bilayers with positive ordering: A new model membrane system
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Prosser RS, Hwang JS, Vold RR. Magnetically aligned phospholipid bilayers with positive ordering: a new model membrane system. Biophys J. 74:1998;2405-2418.
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Prosser, R.S.1
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0032174883
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Characterization of magnetically oriented phospholipid micelles for measurement of dipolar couplings in macromolecules
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in press
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Ottiger M, Bax A. Characterization of magnetically oriented phospholipid micelles for measurement of dipolar couplings in macromolecules. J Biomol NMR. 1998;. in press.
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J Biomol NMR
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Ottiger, M.1
Bax, A.2
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21
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0030612335
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13C couplings in the structure determination of magnetically oriented macromolecules in solution
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of outstanding interest. Residual dipolar couplings are included in the target function of a simulated annealing protocol. Results are shown for a complex of the transcription factor GATA-1 with 16 base-pair DNA, which suggests that in protein - DNA complexes, the magnetic susceptibility tensor is dominated by the DNA. The results indicate that the new constraints obtained from the residual dipolar couplings can be utilized in structure calculations and can improve the quality of structures.
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13C couplings in the structure determination of magnetically oriented macromolecules in solution. of outstanding interest Nat Struct Biol. 4:1997;732-738 Residual dipolar couplings are included in the target function of a simulated annealing protocol. Results are shown for a complex of the transcription factor GATA-1 with 16 base-pair DNA, which suggests that in protein - DNA complexes, the magnetic susceptibility tensor is dominated by the DNA. The results indicate that the new constraints obtained from the residual dipolar couplings can be utilized in structure calculations and can improve the quality of structures.
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(1997)
Nat Struct Biol
, vol.4
, pp. 732-738
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Tjandra, N.1
Omichinski, J.G.2
Gronenborn, A.M.3
Clore, G.M.4
Bax, A.5
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22
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0032012610
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Direct structure refinement against residual dipolar couplings in the presence of rhombicity of unknown magnitude
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Clore GM, Gronenborn AM, Tjandra N. Direct structure refinement against residual dipolar couplings in the presence of rhombicity of unknown magnitude. J Magn Reson. 131:1998;159-162.
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J Magn Reson
, vol.131
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Clore, G.M.1
Gronenborn, A.M.2
Tjandra, N.3
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23
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0030239071
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15N-amino acids
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15N-amino acids. J Biomol NMR. 8:1996;184-192.
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(1996)
J Biomol NMR
, vol.8
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Waugh, D.S.1
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25
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0001050734
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A simple method to distinguish intermonomer nuclear Overhauser effects in homodimeric proteins with C2 symmetry
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of special interest. The authors describe a simple and reliable method for distinguishing intermolecular from intramolecular NOEs in a dimer.
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Walters JK, Matsuo H, Wagner G. A simple method to distinguish intermonomer nuclear Overhauser effects in homodimeric proteins with C2 symmetry. of special interest J Am Chem Soc. 119:1997;5958-5959 The authors describe a simple and reliable method for distinguishing intermolecular from intramolecular NOEs in a dimer.
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(1997)
J Am Chem Soc
, vol.119
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Walters, J.K.1
Matsuo, H.2
Wagner, G.3
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26
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0031297971
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Dimerization of the UmuD' protein in solution and its implications for regulation of SOS mutagenesis
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Ferentz AE, Opperman T, Walker GC, Wagner G. Dimerization of the UmuD' protein in solution and its implications for regulation of SOS mutagenesis. Nat Struct Biol. 4:1997;979-983.
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Nat Struct Biol
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Ferentz, A.E.1
Opperman, T.2
Walker, G.C.3
Wagner, G.4
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27
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0032134275
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An asymmetric deuterium labeling strategy to identify interprotomer and intraprotomer NOEs in ologomeric proteins
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of special interest
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Jasanoff A. An asymmetric deuterium labeling strategy to identify interprotomer and intraprotomer NOEs in ologomeric proteins. of special interest J Biomol NMR. 1998; Jasanoff has developed a procedure for the defined labeling of one protomer in a homotrimer. This can be used to distinguish intraprotomer from interprotomer NOEs.
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(1998)
J Biomol NMR
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Jasanoff, A.1
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28
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0032503612
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Segmental isotope-labeling using peptide splicing for protein NMR
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of outstanding interest. A method is presented based on using the self-splicing protein intein to produce a protein that is labeled in half the sequence.
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Yamazaki T, Otomo T, Oda N, Kyogoku Y, Uegaki K, Ito N, Ishino Y, Nakamura H. Segmental isotope-labeling using peptide splicing for protein NMR. of outstanding interest J Am Chem Soc. 120:1998;5591-5592 A method is presented based on using the self-splicing protein intein to produce a protein that is labeled in half the sequence.
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J Am Chem Soc
, vol.120
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Yamazaki, T.1
Otomo, T.2
Oda, N.3
Kyogoku, Y.4
Uegaki, K.5
Ito, N.6
Ishino, Y.7
Nakamura, H.8
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29
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0030093563
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Multisite band-selective decoupling in proteins
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Kupce E, Wagner G. Multisite band-selective decoupling in proteins. J Magn Reson. 110:1996;309-312.
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J Magn Reson
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0030265965
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Increased sensitivity in HNCA and HNCOCA experiments by selective Cb decoupling
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Matsuo H, Kupce E, Li H, Wagner G. Increased sensitivity in HNCA and HNCOCA experiments by selective Cb decoupling. J Magn Reson. 113:1996;91-96.
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Resolution and sensitivity gain in HCCH-TOCSY experiments by homonuclear Cb decoupling
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Matsuo H, Kupce E, Wagner G. Resolution and sensitivity gain in HCCH-TOCSY experiments by homonuclear Cb decoupling. J Magn Reson. 113:1996;190-194.
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15N isotope editing of biomolecular complexes. Application to a mutant lac repressor headpiece DNA complex
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15N isotope editing of biomolecular complexes. Application to a mutant lac repressor headpiece DNA complex. J Magn Reson. 111:1996;199-203.
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J Magn Reson
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An improved double-tuned and isotope-filtered pulse scheme based on a pulsed field gradient and a wide-band inversion shaped pulse
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Ogura K, Terasawa H, Inagaki F. An improved double-tuned and isotope-filtered pulse scheme based on a pulsed field gradient and a wide-band inversion shaped pulse. J Biomol NMR. 8:1996;492-498.
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0030808350
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Methods for measurement of intermolecular NOEs by multinuclear NMR spectroscopy: Application to a bacteriophage λ N-peptide/boxB RNA complex
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1H one-bond couplings is approximately correlated to the carbon chemical shift was utilized in order to optimize adiabatic inversion pulses for a selection of intermolecular NOEs of a complex between labeled RNA and unlabeled protein.
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1H one-bond couplings is approximately correlated to the carbon chemical shift was utilized in order to optimize adiabatic inversion pulses for a selection of intermolecular NOEs of a complex between labeled RNA and unlabeled protein.
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J Am Chem Soc
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Zwahlen, C.1
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Kupce E, Freeman R. Compensation of spin-spin coupling effects during adiabatic pulses. J Magn Reson. 127:1997;36-48.
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Hwang TL, van Zijl PCM, Garwood M. Broadband adiabatic refocusing without phase distortion. J Magn Reson. 124:1997;250-254.
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