{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,18]],"date-time":"2026-04-18T13:45:30Z","timestamp":1776519930355,"version":"3.51.2"},"reference-count":72,"publisher":"Elsevier BV","issue":"5","license":[{"start":{"date-parts":[[1997,10,1]],"date-time":"1997-10-01T00:00:00Z","timestamp":875664000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Current Opinion in Structural Biology"],"published-print":{"date-parts":[[1997,10]]},"DOI":"10.1016\/s0959-440x(97)80084-x","type":"journal-article","created":{"date-parts":[[2002,7,25]],"date-time":"2002-07-25T10:33:24Z","timestamp":1027593204000},"page":"722-731","source":"Crossref","is-referenced-by-count":144,"title":["Solution NMR spectroscopy beyond 25 kDa"],"prefix":"10.1016","volume":"7","author":[{"given":"Lewis E","family":"Kay","sequence":"first","affiliation":[]},{"given":"Kevin H","family":"Gardner","sequence":"additional","affiliation":[]}],"member":"78","reference":[{"key":"10.1016\/S0959-440X(97)80084-X_BIB1","doi-asserted-by":"crossref","first-page":"674","DOI":"10.1016\/0959-440X(95)80061-1","article-title":"Field gradient techniques in NMR spectroscopy","volume":"5","author":"Kay","year":"1995","journal-title":"Curr Opin Struct Biol"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB2","doi-asserted-by":"crossref","first-page":"738","DOI":"10.1016\/S0959-440X(94)90173-2","article-title":"Multidimensional nuclear magnetic resonance methods for protein studies","volume":"4","author":"Bax","year":"1994","journal-title":"Curr Opin Struct Biol"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB3","doi-asserted-by":"crossref","first-page":"88","DOI":"10.1006\/jmrb.1995.1063","article-title":"Three-dimensional solid-state NMR experiment that correlates the chemical shift and dipolar coupling frequencies of two heteronuclei","volume":"107","author":"Ramamoorthy","year":"1995","journal-title":"J Magn Reson Series B"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB4","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1007\/BF00410323","article-title":"Prospects for resonance assignments in multidimensional solid-state NMR spectra of uniformly labeled proteins","volume":"8","author":"Tycko","year":"1996","journal-title":"J Biomol NMR"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB5","author":"W\u00fcthrich","year":"1986"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB6","doi-asserted-by":"crossref","first-page":"1249","DOI":"10.1126\/science.161.3847.1249","article-title":"High resolution nuclear magnetic resonance spectra of selectively deuterated staphylococcal nuclease","volume":"161","author":"Markley","year":"1968","journal-title":"Science"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB7","doi-asserted-by":"crossref","first-page":"795","DOI":"10.1126\/science.161.3843.795","article-title":"Proton magnetic resonance of proteins fully deuterated except for 1H-leucine side-chains","volume":"161","author":"Crespi","year":"1968","journal-title":"Science"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB8","doi-asserted-by":"crossref","first-page":"142","DOI":"10.1021\/bi00401a022","article-title":"NMR sequential assignment of Escherichia coli thioredoxin utilizing random fractional deuteration","volume":"27","author":"LeMaster","year":"1988","journal-title":"Biochemistry"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB9","first-page":"735","article-title":"The solution structure of the trp repressor\u2014operator DNA complex","volume":"229","author":"Zhang","year":"1994","journal-title":"J Mol Biol"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB10","doi-asserted-by":"crossref","first-page":"1316","DOI":"10.1021\/ja00785a050","article-title":"Studies of macromolecular structure by 13C nuclear magnetic resonance. II. A specific labeling approach to the study of histidine residues in proteins","volume":"95","author":"Browne","year":"1973","journal-title":"J Am Chem Soc"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB11","doi-asserted-by":"crossref","first-page":"4369","DOI":"10.1021\/ja00063a068","article-title":"13C line narrowing by 2H decoupling in 2H\/13C\/15N-enriched proteins. Applications to triple resonance 4D J-connectivity of sequential amides","volume":"115","author":"Grzesiek","year":"1993","journal-title":"J Am Chem Soc"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB12_1","doi-asserted-by":"crossref","first-page":"1101","DOI":"10.1006\/jmbi.1996.0699","article-title":"Characterizing the use of perdeuteration in NMR studies of large proteins: 13C, 15N and 1H assignments of human carbonic anhydrase II","volume":"264","author":"Venters","year":"1996","journal-title":"J Mol Biol"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB13","doi-asserted-by":"crossref","first-page":"192","DOI":"10.1006\/jmrb.1994.1122","article-title":"Effect of deuteration on the amide proton relaxation rates in proteins. Heteronuclear NMR experiments on villin 14T","volume":"105","author":"Markus","year":"1994","journal-title":"J Magn Reson Series B"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB14","doi-asserted-by":"crossref","first-page":"6464","DOI":"10.1021\/ja00093a069","article-title":"An HNCA pulse scheme for the backbone assignment of 15N, 13C, 2H labeled proteins: application to a 37 kDa trp repressor\u2014DNA complex","volume":"116","author":"Yamazaki","year":"1994","journal-title":"J Am Chem Soc"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB15","doi-asserted-by":"crossref","first-page":"11655","DOI":"10.1021\/ja00105a005","article-title":"A suite of triple resonance NMR experiments for the backbone assignment of 15N, 13C, 2H labeled proteins with high sensitivity","volume":"116","author":"Yamazaki","year":"1994","journal-title":"J Am Chem Soc"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB16_1","doi-asserted-by":"crossref","first-page":"1389","DOI":"10.1021\/bi9624806","article-title":"Global folds of highly deuterated, methyl protonated proteins by multidimensional NMR","volume":"36","author":"Gardner","year":"1997","journal-title":"Biochemistry"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB17","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1006\/jmrb.1996.0018","article-title":"A sensitive HN(CA)CO experiment for deuterated proteins","volume":"110","author":"Matsuo","year":"1996","journal-title":"J Magn Reson Series B"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB18","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1007\/BF00211761","article-title":"The use of heteronuclear cross-polarization for backbone assignment of 2H, 15N and 13C labeled proteins: a pulse scheme for triple-resonance 4D correlation of sequential amide protons and 15N","volume":"5","author":"Shirakawa","year":"1995","journal-title":"J Biomol NMR"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB19","doi-asserted-by":"crossref","first-page":"194","DOI":"10.1006\/jmrb.1996.0082","article-title":"Use of Selective C\u03b1 pulses for improvement of HN(CA)CO-D and HN(COCA)NH-D experiments","volume":"111","author":"Matsuo","year":"1996","journal-title":"J Magn Reson Series B"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB20","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1006\/jmrb.1996.0117","article-title":"Amino-acid type identification for deuterated proteins with a \u03b2-carbon-edited HNCOCACB experiment","volume":"112","author":"D\u00f6tsch","year":"1996","journal-title":"J Magn Reson Series B"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB21","doi-asserted-by":"crossref","first-page":"214","DOI":"10.1006\/jmre.1996.7497","article-title":"An efficient HN(CA)NH pulse scheme for triple-resonance 4D correlation of sequential amide protons and nitrogen-15 in deuterated proteins","volume":"124","author":"Ikegami","year":"1997","journal-title":"J Magn Reson"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB22_1","doi-asserted-by":"crossref","first-page":"872","DOI":"10.1021\/ja962945f","article-title":"Assignment of backbone resonances for larger proteins using the 13C-1H coherence of 1H\u03b1, 2H, 13C and 15N labeled sample","volume":"119","author":"Yamazaki","year":"1997","journal-title":"J Am Chem Soc"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB23","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1017\/S0033583500004029","article-title":"Proton-detected heteronuclear edited and correlated nuclear magnetic resonance and nuclear Overhauser effect in solution","volume":"19","author":"Griffey","year":"1987","journal-title":"Quart Rev Biophys"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB24","doi-asserted-by":"crossref","first-page":"335","DOI":"10.1007\/BF00197815","article-title":"Spin-locked multiple quantum coherence for signal enhancement in heteronuclear multidimensional NMR experiments","volume":"6","author":"Grzesiek","year":"1995","journal-title":"J Biomol NMR"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB25_1","doi-asserted-by":"crossref","DOI":"10.1021\/ja964379u","article-title":"Multiple quantum coherence leads to a sensitivity enhancement of up to a factor of three for CH and CH2 correlations in uniformly 13C labeled RNA","author":"Marino","year":"1997","journal-title":"J Am Chem Soc"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB26","doi-asserted-by":"crossref","first-page":"4187","DOI":"10.1021\/ja00119a042","article-title":"Assignment of side-chain 13C resonances in perdeuterated proteins","volume":"117","author":"Farmer","year":"1995","journal-title":"J Am Chem Soc"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB27","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1007\/BF00190457","article-title":"Assignment of aliphatic side-chain 1HN\/15N resonances in perdeuterated proteins","volume":"7","author":"Farmer","year":"1996","journal-title":"J Biomol NMR"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB28_1","doi-asserted-by":"crossref","first-page":"407","DOI":"10.1021\/ja952207b","article-title":"An approach to the structure determination of larger proteins using triple resonance NMR experiments in conjunction with random fractional deuteration","volume":"118","author":"Nietlispach","year":"1996","journal-title":"J Am Chem Soc"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB29_1","doi-asserted-by":"crossref","first-page":"6570","DOI":"10.1021\/ja960627a","article-title":"Assignment of 15N, 13C\u03b1, 13C\u03b2 and HN resonances in an 15N, 13C, 2H labeled 64 kDa trp repressor\u2014operator complex using triple resonance NMR spectroscopy and 2H-decoupling","volume":"118","author":"Shan","year":"1996","journal-title":"J Am Chem Soc"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB30","doi-asserted-by":"crossref","first-page":"1223","DOI":"10.1006\/jmbi.1997.0915","article-title":"Characterization of NADP+ binding to perdeuterated MurB: backbone atom NMR assignments and chemical-shift changes","volume":"267","author":"Constantine","year":"1997","journal-title":"J Mol Biol"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB31_1","doi-asserted-by":"crossref","first-page":"2517","DOI":"10.1021\/bi962924y","article-title":"Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate: sugar phosphotransferase system by multi-dimensional NMR","volume":"36","author":"Garrett","year":"1997","journal-title":"Biochemistry"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB32","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1038\/nsb0197-9","article-title":"Large modular proteins by NMR","volume":"4","author":"McEvoy","year":"1997","journal-title":"Nat Struct Biol"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB33","doi-asserted-by":"crossref","first-page":"2320","DOI":"10.1021\/ja00215a063","article-title":"Delineation of \u03b1-helical domains in deuterated staphylococcal nuclease by 2D NOE NMR spectroscopy","volume":"110","author":"Torchia","year":"1988","journal-title":"J Am Chem Soc"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB34","doi-asserted-by":"crossref","first-page":"9592","DOI":"10.1021\/ja00142a039","article-title":"Use of 1HN\u20141HN NOEs to determine protein global folds in perdeuterated proteins","volume":"117","author":"Venters","year":"1995","journal-title":"J Am Chem Soc"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB35","doi-asserted-by":"crossref","first-page":"9594","DOI":"10.1021\/ja00142a040","article-title":"Four-dimensional 15N separated NOESY of slowly tumbling perdeuterated 15N-enriched proteins. Application to HIV-1 Nef","volume":"117","author":"Grzesiek","year":"1995","journal-title":"J Am Chem Soc"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB36_1","doi-asserted-by":"crossref","first-page":"6800","DOI":"10.1021\/ja9604875","article-title":"Incorporation of 1H\/13C\/15N-(Ile,Leu,Val) into a perdeuterated, 15N-labeled protein: potential in structure determination of large proteins by NMR","volume":"118","author":"Metzler","year":"1996","journal-title":"J Am Chem Soc"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB37_1","doi-asserted-by":"crossref","first-page":"360","DOI":"10.1007\/BF00410335","article-title":"An approach to global fold determination using limited NMR data from larger proteins selectively protonated at specific residues","volume":"8","author":"Smith","year":"1996","journal-title":"J Biomol NMR"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB38_1","doi-asserted-by":"crossref","first-page":"627","DOI":"10.1006\/jmbi.1996.0603","article-title":"Selective methyl group protonation of perdeuterated proteins","volume":"263","author":"Rosen","year":"1996","journal-title":"J Mol Biol"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB39","doi-asserted-by":"crossref","first-page":"351","DOI":"10.1007\/BF00410333","article-title":"A (H)C(CO)NH-TOCSY pulse scheme for sequential assignment of protonated methyl groups in otherwise deuterated 15N,13C labeled proteins","volume":"8","author":"Gardner","year":"1996","journal-title":"J Biomol NMR"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB40_1","doi-asserted-by":"crossref","DOI":"10.1021\/ja9706514","article-title":"Production and incorporation of 15N, 13C, 2H (1H-\u03b41 methyl) isoleucine into proteins for multidimensional NMR studies","author":"Gardner","year":"1997","journal-title":"J Am Chem Soc"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB41_1","doi-asserted-by":"crossref","first-page":"995","DOI":"10.1038\/nsb1296-995","article-title":"Localizing the NADP+ binding site on the MurB enzyme by NMR","volume":"3","author":"Farmer","year":"1996","journal-title":"Nat Struct Biol"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB42","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1006\/jmre.1997.1116","article-title":"Improvements and extensions in the conformational database potential for the refinement of NMR and X-ray structures of proteins and nucleic acids","volume":"125","author":"Kuszewski","year":"1997","journal-title":"J Magn Reson"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB43","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1006\/jmrb.1995.1017","article-title":"The impact of direct refinement against 13C\u03b1 and 13C\u03b2 chemical shifts on protein structure determination by NMR","volume":"106","author":"Kuszewski","year":"1995","journal-title":"J Magn Reson Series B"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB44","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1006\/jmrb.1995.0016","article-title":"Statistical basis for the use of 13C\u03b1 chemical shifts in protein structure refinement","volume":"109","author":"Luginb\u00fchl","year":"1995","journal-title":"J Magn Reson Series B"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB45","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1007\/BF00175245","article-title":"The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data","volume":"4","author":"Wishart","year":"1994","journal-title":"J Biomol NMR"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB46","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1007\/BF00211749","article-title":"Chemical shifts and three-dimensional protein structures","volume":"5","author":"Oldfield","year":"1995","journal-title":"J Biomol NMR"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB47_1","doi-asserted-by":"crossref","first-page":"483","DOI":"10.1038\/nsb0697-483","article-title":"Solution structure of an rRNA methyltransferase (ErmAm) that confers MLS antibiotic resistance","volume":"4","author":"Yu","year":"1997","journal-title":"Nat Struct Biol"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB48","doi-asserted-by":"crossref","first-page":"584","DOI":"10.1038\/378584a0","article-title":"Structure and ligand recognition of the phosphotyrosine binding domain of Shc","volume":"378","author":"Zhou","year":"1995","journal-title":"Nature"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB49","doi-asserted-by":"crossref","first-page":"335","DOI":"10.1038\/381335a0","article-title":"X-ray and NMR structure of human BCL-xL, an inhibitor of programmed cell death","volume":"381","author":"Muchmore","year":"1996","journal-title":"Nature"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB50","doi-asserted-by":"crossref","first-page":"983","DOI":"10.1126\/science.275.5302.983","article-title":"Structure of Bcl-xL\u2014Bak peptide complex: recognition between regulators of apoptosis","volume":"275","author":"Sattler","year":"1997","journal-title":"Science"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB51","doi-asserted-by":"crossref","first-page":"192","DOI":"10.1016\/0009-2614(82)83585-9","article-title":"Dipolar magnetic field effects in NMR spectroscopy","volume":"87","author":"Gayathra","year":"1982","journal-title":"Chem Phys Lett"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB52","doi-asserted-by":"crossref","first-page":"9279","DOI":"10.1073\/pnas.92.20.9279","article-title":"Nuclear magnetic dipole interactions in field-oriented proteins: information for structure determination in solution","volume":"92","author":"Tolman","year":"1995","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB53_1","doi-asserted-by":"crossref","first-page":"6264","DOI":"10.1021\/ja960106n","article-title":"Magnetic field dependence of nitrogen\u2014proton J splittings in 15N enriched human ubiquitin resulting from relaxation interference and residual dipolar coupling","volume":"118","author":"Tjandra","year":"1996","journal-title":"J Am Chem Soc"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB54_1","doi-asserted-by":"crossref","first-page":"292","DOI":"10.1038\/nsb0497-292","article-title":"NMR evidence for slow collective motions in cyanometmyoglobin","volume":"4","author":"Tolman","year":"1997","journal-title":"Nat Struct Biol"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB55_1","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1006\/jmrb.1996.0138","article-title":"A quantitative J-correlation experiment for the accurate measurement of one-bond amide 15N-1H couplings in proteins","volume":"112","author":"Tolman","year":"1996","journal-title":"J Magn Reson Series B"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB56","doi-asserted-by":"crossref","first-page":"512","DOI":"10.1006\/jmre.1996.1088","article-title":"Measurement of dipolar contributions to 1JCH splittings from magnetic-field dependence of J modulation in two-dimensional NMR spectra","volume":"124","author":"Tjandra","year":"1997","journal-title":"J Magn Reson"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB57_1","doi-asserted-by":"crossref","DOI":"10.1038\/nsb0997-732","article-title":"Using dipolar 1H\u201415N and 1H\u201413C couplings in the structure determination of magnetically oriented macromolecules in solution","author":"Tjandra","year":"1997","journal-title":"Nat Struct Biol"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB58","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1016\/0958-1669(93)90002-E","article-title":"Dynamic properties of proteins from NMR spectroscopy","volume":"4","author":"Palmer","year":"1993","journal-title":"Curr Opin Biotechnol"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB59_1","doi-asserted-by":"crossref","first-page":"443","DOI":"10.1038\/nsb0697-443","article-title":"Defining long range order in NMR structure determination by diffusion induced relaxation anisotropy","volume":"4","author":"Tjandra","year":"1997","journal-title":"Nat Struct Biol"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB60_1","doi-asserted-by":"crossref","first-page":"1230","DOI":"10.1126\/science.276.5316.1230","article-title":"Direct measurement of angles between bond vectors in high resolution NMR","volume":"276","author":"Reif","year":"1997","journal-title":"Science"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB61","doi-asserted-by":"crossref","first-page":"170","DOI":"10.1006\/jmbi.1997.0953","article-title":"Characterization of long range structure in the denatured state of staphylococcal nuclease. II. Distance restraints from paramagnetic relaxation and calculation of an ensemble of structures","volume":"268","author":"Gillespie","year":"1997","journal-title":"J Mol Biol"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB62","doi-asserted-by":"crossref","DOI":"10.1023\/A:1018354712430","article-title":"Pulse schemes for the measurement of 3JC\u2032C\u03b3 and 3JNC\u03b3 scalar couplings in 15N,13C uniformly labeled proteins","author":"Konrat","year":"1997","journal-title":"J Biomol NMR"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB63","doi-asserted-by":"crossref","first-page":"1803","DOI":"10.1021\/ja963625z","article-title":"Two-dimensional NMR methods for determining \u03c71 angles of aromatic residues in proteins from three-bond JC\u2032C\u03b3 and JNC\u03b3 couplings","volume":"119","author":"Hu","year":"1997","journal-title":"J Am Chem Soc"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB64","doi-asserted-by":"crossref","first-page":"6360","DOI":"10.1021\/ja970067v","article-title":"Determination of \u03c6 and \u03c71 angles in proteins from 13C\ue5f813C three-bond J couplings measured by three-dimensional heteronuclear NMR. How planar is the peptide bond?","volume":"119","author":"Hu","year":"1997","journal-title":"J Am Chem Soc"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB65_1","doi-asserted-by":"crossref","first-page":"5055","DOI":"10.1021\/ja970034f","article-title":"Determination of homonuclear 13C\ue5f813C J couplings between aliphatic carbon atoms in perdeuterated proteins","volume":"119","author":"Hennig","year":"1997","journal-title":"J Am Chem Soc"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB66_1","doi-asserted-by":"crossref","first-page":"6711","DOI":"10.1021\/ja970224q","article-title":"Methods for measurement of intermolecular NOEs by multinuclear NMR spectroscopy: application to a bacteriophage I N-peptide\/box B RNA complex","volume":"119","author":"Zwahlen","year":"1997","journal-title":"J Am Chem Soc"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB67_1","doi-asserted-by":"crossref","first-page":"1531","DOI":"10.1126\/science.274.5292.1531","article-title":"Discovering high-affinity ligands for proteins: SAR by NMR","volume":"274","author":"Shuker","year":"1996","journal-title":"Science"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB68","doi-asserted-by":"crossref","first-page":"4393","DOI":"10.1021\/bi970221q","article-title":"Identification by NMR of the binding surface for the histidine-containing phosphocarrier protein HPr on the N-terminal domain of enzyme I of the Escherichia coli phosphotransferase system","volume":"36","author":"Garrett","year":"1997","journal-title":"Biochemistry"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB69","doi-asserted-by":"crossref","first-page":"7929","DOI":"10.1021\/ja961274i","article-title":"Preparation of specifically deuterated RNA for NMR studies using a combination of chemical and enzymatic synthesis","volume":"118","author":"Tolbert","year":"1996","journal-title":"J Am Chem Soc"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB70","doi-asserted-by":"crossref","first-page":"S40","DOI":"10.1002\/(SICI)1097-458X(199612)34:13<S40::AID-OMR43>3.0.CO;2-Y","article-title":"C5'-methylene proton signal assignment of DNA\/RNA oligomers labeled with C5'-monodeuterated nucleosides by 1H-31P HSQC spectroscopy","volume":"34","author":"Ono","year":"1996","journal-title":"Magn Reson Chem"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB71","doi-asserted-by":"crossref","first-page":"4836","DOI":"10.1093\/nar\/24.23.4836","article-title":"Improved large scale culture of Methylophilus methylotrophus for 13C\/15N labeling and random fractional deuteration of ribonucleotides","volume":"24","author":"Batey","year":"1996","journal-title":"Nucleic Acids Res"},{"key":"10.1016\/S0959-440X(97)80084-X_BIB72","doi-asserted-by":"crossref","first-page":"1404","DOI":"10.1093\/nar\/22.8.1404","article-title":"The differences in the T2 relaxation rates of the protons in the partially deuterated and fully protonated sugar residues in a large oligo-DNA (NMR-window) gives complementary structural information","volume":"22","author":"Agback","year":"1994","journal-title":"Nucleic Acids Res"}],"container-title":["Current Opinion in Structural Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0959440X9780084X?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0959440X9780084X?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2019,5,2]],"date-time":"2019-05-02T21:20:32Z","timestamp":1556832032000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0959440X9780084X"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1997,10]]},"references-count":72,"journal-issue":{"issue":"5","published-print":{"date-parts":[[1997,10]]}},"alternative-id":["S0959440X9780084X"],"URL":"https:\/\/doi.org\/10.1016\/s0959-440x(97)80084-x","relation":{},"ISSN":["0959-440X"],"issn-type":[{"value":"0959-440X","type":"print"}],"subject":[],"published":{"date-parts":[[1997,10]]}}}