{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,22]],"date-time":"2026-10-22T22:02:40Z","timestamp":1792706560844,"version":"4.5.0"},"reference-count":64,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2014,10,1]],"date-time":"2014-10-01T00:00:00Z","timestamp":1412121600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["GM088204"],"award-info":[{"award-number":["GM088204"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Magnetic Resonance"],"published-print":{"date-parts":[[2014,10]]},"DOI":"10.1016\/j.jmr.2014.08.007","type":"journal-article","created":{"date-parts":[[2014,8,25]],"date-time":"2014-08-25T02:00:17Z","timestamp":1408932017000},"page":"118-127","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":67,"special_numbering":"C","title":["Probing membrane protein structure using water polarization transfer solid-state NMR"],"prefix":"10.1016","volume":"247","author":[{"given":"Jonathan K.","family":"Williams","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mei","family":"Hong","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jmr.2014.08.007_b0005","doi-asserted-by":"crossref","first-page":"1207","DOI":"10.1098\/rstb.2004.1499","article-title":"Protein hydration dynamics in solution: a critical survey","volume":"359","author":"Halle","year":"2004","journal-title":"Philos. Trans. R. Soc. London, B"},{"key":"10.1016\/j.jmr.2014.08.007_b0010","doi-asserted-by":"crossref","first-page":"1543","DOI":"10.1002\/pro.5560011203","article-title":"Internal water molecules and H-bonding in biological macromolecules: a review of structural features with functional implications","volume":"1","author":"Meyer","year":"1992","journal-title":"Protein Sci."},{"key":"10.1016\/j.jmr.2014.08.007_b0015","doi-asserted-by":"crossref","first-page":"1277","DOI":"10.1098\/rstb.2004.1504","article-title":"Probing the role of water in protein conformation and function","volume":"359","author":"Rand","year":"2004","journal-title":"Philos. Trans. R. Soc. London, B"},{"key":"10.1016\/j.jmr.2014.08.007_b0020","doi-asserted-by":"crossref","first-page":"4300","DOI":"10.1021\/jp070104x","article-title":"Proton solvation and transport in aqueous and biomolecular systems: insights from computer simulations","volume":"111","author":"Swanson","year":"2007","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.jmr.2014.08.007_b0025","doi-asserted-by":"crossref","first-page":"974","DOI":"10.1126\/science.1948083","article-title":"Protein hydration in aqueous solution","volume":"254","author":"Otting","year":"1991","journal-title":"Science"},{"key":"10.1016\/j.jmr.2014.08.007_b0030","doi-asserted-by":"crossref","first-page":"1813","DOI":"10.1126\/science.7892604","article-title":"Demonstration of positionally disordered water within a protein hydrophobic cavity by NMR","volume":"267","author":"Ernst","year":"1995","journal-title":"Science"},{"key":"10.1016\/j.jmr.2014.08.007_b0035","doi-asserted-by":"crossref","first-page":"7221","DOI":"10.1021\/ja00229a051","article-title":"Solid-state NMR detection of proton exchange between the bacteriorhodopsin Schiff base and bulk water","volume":"110","author":"Harbison","year":"1988","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jmr.2014.08.007_b0040","doi-asserted-by":"crossref","first-page":"8246","DOI":"10.1021\/ja060866q","article-title":"Investigation of dipolar-mediated water\u2013protein interactions in microcrystalline Crh by solid-state NMR spectroscopy","volume":"128","author":"Lesage","year":"2006","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jmr.2014.08.007_b0045","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1103\/PhysRev.144.321","article-title":"Spin\u2013spin relaxation in LaF3","volume":"144","author":"Goldman","year":"1966","journal-title":"Phys. Rev."},{"key":"10.1016\/j.jmr.2014.08.007_b0050","doi-asserted-by":"crossref","first-page":"5043","DOI":"10.1021\/ja972655e","article-title":"A novel tool for probing membrane protein structure: solid-state NMR with proton spin diffusion and X-nucleus detection","volume":"120","author":"Kumashiro","year":"1998","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jmr.2014.08.007_b0055","doi-asserted-by":"crossref","first-page":"170","DOI":"10.1021\/ja806306e","article-title":"Structural rearrangements of membrane proteins probed by water-edited solid-state NMR spectroscopy","volume":"131","author":"Ader","year":"2009","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jmr.2014.08.007_b0060","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1016\/j.jmr.2008.10.001","article-title":"2D 1H\u201331P solid-state NMR studies of the dependence of inter-bilayer water dynamics on lipid headgroup structure and membrane peptides","volume":"196","author":"Doherty","year":"2009","journal-title":"J. Magn. Reson."},{"key":"10.1016\/j.jmr.2014.08.007_b0065","doi-asserted-by":"crossref","first-page":"874","DOI":"10.1021\/ja017001r","article-title":"Membrane protein topology probed by 1H spin diffusion from lipids using solid-state NMR spectroscopy","volume":"124","author":"Huster","year":"2002","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jmr.2014.08.007_b0070","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1023\/A:1011251924874","article-title":"Dipolar filtered 1H\u201313C heteronuclear correlation spectroscopy for resonance assignment of proteins","volume":"20","author":"Yao","year":"2001","journal-title":"J. Biomol. NMR"},{"key":"10.1016\/j.jmr.2014.08.007_b0075","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1006\/jmre.2001.2285","article-title":"Medium- and long-distance 1H\u201313C heteronuclear correlation NMR in solids","volume":"149","author":"Yao","year":"2001","journal-title":"J. Magn. Reson."},{"key":"10.1016\/j.jmr.2014.08.007_b0080","doi-asserted-by":"crossref","first-page":"4063","DOI":"10.1021\/jp912283r","article-title":"Water\u2013protein interactions of an arginine-rich membrane peptide in lipid bilayers investigated by solid-state nuclear magnetic resonance spectroscopy","volume":"114","author":"Li","year":"2010","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.jmr.2014.08.007_b0085","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1016\/j.ssnmr.2005.08.007","article-title":"A 1D sensitivity-enhanced 1H spin diffusion experiment for determining membrane protein topology","volume":"29","author":"Luo","year":"2006","journal-title":"Solid State Nucl. Magn. Reson."},{"key":"10.1016\/j.jmr.2014.08.007_b0090","doi-asserted-by":"crossref","first-page":"1700","DOI":"10.1063\/1.1485062","article-title":"C-13 nuclear Overhauser polarization nuclear magnetic resonance in rotating solids: replacement of cross polarization in uniformly C-13 labeled molecules with methyl groups","volume":"117","author":"Takegoshi","year":"2002","journal-title":"J. Chem. Phys."},{"key":"10.1016\/j.jmr.2014.08.007_b0095","doi-asserted-by":"crossref","first-page":"30","DOI":"10.1002\/mrm.1910350106","article-title":"Proton exchange rates from amino acid side chains \u2013 implications for image contrast","volume":"35","author":"Liepinsh","year":"1996","journal-title":"Magn. Reson. Med."},{"key":"10.1016\/j.jmr.2014.08.007_b0100","doi-asserted-by":"crossref","first-page":"3923","DOI":"10.1021\/ja00907a004","article-title":"Kinetics of proton exchange in aqueous solutions of acetate buffer","volume":"85","author":"Luz","year":"1963","journal-title":"J. Am. Chem. Soc"},{"key":"10.1016\/j.jmr.2014.08.007_b0105","doi-asserted-by":"crossref","first-page":"386","DOI":"10.1016\/0031-8914(49)90114-7","article-title":"On the interaction of nuclear spins in a crystalline lattice","volume":"15","author":"Bloembergen","year":"1949","journal-title":"Physica"},{"key":"10.1016\/j.jmr.2014.08.007_b0110","series-title":"Multidimensional Solid-State NMR and Polymers","author":"Schmidt-Rohr","year":"1994"},{"key":"10.1016\/j.jmr.2014.08.007_b0115","series-title":"The Nuclear Overhauser Effect: Chemical Applications","author":"Noggle","year":"1971"},{"key":"10.1016\/j.jmr.2014.08.007_b0120","doi-asserted-by":"crossref","first-page":"559","DOI":"10.1103\/PhysRev.99.559","article-title":"Relaxation processes in a system of two spins","volume":"99","author":"Solomon","year":"1955","journal-title":"Phys. Rev."},{"key":"10.1016\/j.jmr.2014.08.007_b0125","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1007\/s10858-005-1718-z","article-title":"Detection of dynamic water molecules in a microcrystalline sample of the SH3 domain of alpha-spectrin by MAS solid-state NMR","volume":"31","author":"Chevelkov","year":"2005","journal-title":"J. Biomol. NMR"},{"key":"10.1016\/j.jmr.2014.08.007_b0130","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1007\/s10858-009-9374-3","article-title":"Characterization of different water pools in solid-state NMR protein samples","volume":"45","author":"B\u00f6ckmann","year":"2009","journal-title":"J. Biomol. NMR"},{"key":"10.1016\/j.jmr.2014.08.007_b0135","doi-asserted-by":"crossref","first-page":"10399","DOI":"10.1021\/ja504108h","article-title":"Water\u2013polysaccharide interactions in the primary cell wall of Arabidopsis thaliana from polarization transfer solid-state NMR","volume":"136","author":"White","year":"2014","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jmr.2014.08.007_b0140","doi-asserted-by":"crossref","first-page":"2611","DOI":"10.1021\/ja4121956","article-title":"Conformation and lipid interaction of the fusion peptide of the paramyxovirus PIV5 in anionic and negative-curvature membranes from solid-state NMR","volume":"136","author":"Yao","year":"2014","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jmr.2014.08.007_b0145","doi-asserted-by":"crossref","first-page":"13336","DOI":"10.1021\/ja036720y","article-title":"Water\u2013protein interactions in microcrystalline Crh measured by H-1\u2013C-13 solid-state NMR spectroscopy","volume":"125","author":"Lesage","year":"2003","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jmr.2014.08.007_b0150","doi-asserted-by":"crossref","first-page":"5851","DOI":"10.1002\/anie.200801110","article-title":"Polarization transfer over the water\u2013protein interface in solids","volume":"47","author":"Lesage","year":"2008","journal-title":"Angew. Chem., Int. Ed. Engl."},{"key":"10.1016\/j.jmr.2014.08.007_b0155","doi-asserted-by":"crossref","first-page":"14222","DOI":"10.1021\/ja037559u","article-title":"High-sensitivity observation of dipolar exchange and NOEs between exchangeable protons in proteins by 3D solid-state NMR spectroscopy","volume":"125","author":"Paulson","year":"2003","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jmr.2014.08.007_b0160","doi-asserted-by":"crossref","first-page":"17580","DOI":"10.1073\/pnas.1009369107","article-title":"Protein\u2013ice interaction of an antifreeze protein observed with solid-state NMR","volume":"107","author":"Siemer","year":"2010","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jmr.2014.08.007_b0165","doi-asserted-by":"crossref","first-page":"2378","DOI":"10.1021\/ja9096219","article-title":"Conformational changes of an ion channel detected through water\u2013protein interactions using solid-state NMR spectroscopy","volume":"132","author":"Luo","year":"2010","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jmr.2014.08.007_b0170","doi-asserted-by":"crossref","first-page":"2000","DOI":"10.1021\/ja411450y","article-title":"Quantitative analysis of the water occupancy around the selectivity filter of a K+ channel in different gating modes","volume":"136","author":"Weingarth","year":"2014","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jmr.2014.08.007_b0175","doi-asserted-by":"crossref","first-page":"14753","DOI":"10.1021\/ja307453v","article-title":"Hydrogen-bonding partner of the proton-conducting histidine in the influenza M2 proton channel revealed from 1H chemical shifts","volume":"134","author":"Hong","year":"2012","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jmr.2014.08.007_b0180","doi-asserted-by":"crossref","first-page":"509","DOI":"10.1126\/science.1191750","article-title":"Insight into the mechanism of the influenza A proton channel from a structure in a lipid bilayer","volume":"330","author":"Sharma","year":"2010","journal-title":"Science"},{"key":"10.1016\/j.jmr.2014.08.007_b0185","doi-asserted-by":"crossref","first-page":"505","DOI":"10.1126\/science.1191714","article-title":"Mechanisms of proton conduction and gating in influenza M2 proton channels from solid-state NMR","volume":"330","author":"Hu","year":"2010","journal-title":"Science"},{"key":"10.1016\/j.jmr.2014.08.007_b0190","doi-asserted-by":"crossref","first-page":"459","DOI":"10.1002\/anie.200602139","article-title":"Secondary structure, dynamics, and topology of a seven-helix receptor in native membranes, studied by solid-state NMR spectroscopy","volume":"46","author":"Etzkorn","year":"2007","journal-title":"Angew. Chem., Int. Ed. Engl."},{"key":"10.1016\/j.jmr.2014.08.007_b0195","doi-asserted-by":"crossref","first-page":"1623","DOI":"10.1002\/pro.2368","article-title":"Conformational analysis of the full-length M2 protein of the influenza A virus using solid-state NMR","volume":"22","author":"Liao","year":"2013","journal-title":"Protein Sci."},{"key":"10.1016\/j.jmr.2014.08.007_b0200","doi-asserted-by":"crossref","first-page":"7899","DOI":"10.1021\/bi0356101","article-title":"Solid-state NMR spin diffusion for measurement of membrane-bound peptide structure: gramicidin A","volume":"43","author":"Gallagher","year":"2004","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmr.2014.08.007_b0205","doi-asserted-by":"crossref","first-page":"5624","DOI":"10.1002\/anie.201311203","article-title":"Conformation and topology of diacylglycerol kinase in E. coli membranes revealed by solid-state NMR spectroscopy","author":"Chen","year":"2014","journal-title":"Angew. Chem., Int. Ed."},{"key":"10.1016\/j.jmr.2014.08.007_b0210","doi-asserted-by":"crossref","first-page":"1302","DOI":"10.1002\/anie.201004422","article-title":"Conformation of a seven-helical transmembrane photosensor in the lipid environment","volume":"50","author":"Shi","year":"2011","journal-title":"Angew. Chem., Int. Ed."},{"key":"10.1016\/j.jmr.2014.08.007_b0215","doi-asserted-by":"crossref","first-page":"L23","DOI":"10.1016\/j.bpj.2011.06.035","article-title":"Site-specific solid-state NMR detection of hydrogen-deuterium exchange reveals conformational changes in a 7-helical transmembrane protein","volume":"101","author":"Wang","year":"2011","journal-title":"Biophys. J."},{"key":"10.1016\/j.jmr.2014.08.007_b0220","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1016\/S0926-2040(96)01260-X","article-title":"Hydrogen exchange in the lipid bilayer-bound gramicidin channel","volume":"7","author":"Huo","year":"1996","journal-title":"Solid State Nucl. Magn. Reson."},{"key":"10.1016\/j.jmr.2014.08.007_b0225","doi-asserted-by":"crossref","first-page":"1179","DOI":"10.1016\/S0006-3495(99)77282-6","article-title":"Solid-state NMR and hydrogen-deuterium exchange in a bilayer-solubilized peptide: structural and mechanistic implications","volume":"76","author":"Cotten","year":"1999","journal-title":"Biophys. J."},{"key":"10.1016\/j.jmr.2014.08.007_b0230","doi-asserted-by":"crossref","first-page":"2597","DOI":"10.1110\/ps.03168503","article-title":"Initial structural and dynamic characterization of the M2 protein transmembrane and amphipathic helices in lipid bilayers","volume":"12","author":"Tian","year":"2003","journal-title":"Protein Sci."},{"key":"10.1016\/j.jmr.2014.08.007_b0235","doi-asserted-by":"crossref","first-page":"4740","DOI":"10.1039\/b005319h","article-title":"Temperature-dependent self-diffusion coefficients of water and six selected molecular liquids for calibration in accurate 1H NMR PFG measurements","volume":"2","author":"Holz","year":"2000","journal-title":"Phys. Chem. Chem. Phys."},{"key":"10.1016\/j.jmr.2014.08.007_b0240","doi-asserted-by":"crossref","first-page":"4175","DOI":"10.1021\/ja3112912","article-title":"Nonlinear scaling of surface water diffusion with bulk water viscosity of crowded solutions","volume":"135","author":"Franck","year":"2013","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jmr.2014.08.007_b0245","doi-asserted-by":"crossref","first-page":"4641","DOI":"10.1021\/ja809259q","article-title":"Overhauser dynamic nuclear polarization to study local water dynamics","volume":"131","author":"Armstrong","year":"2009","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jmr.2014.08.007_b0250","doi-asserted-by":"crossref","first-page":"989","DOI":"10.1021\/bi101795q","article-title":"Structure and interactions of plant cell-wall polysaccharides by two- and three-dimensional magic-angle-spinning solid-state NMR","volume":"50","author":"Dick-P\u00e9rez","year":"2011","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmr.2014.08.007_b0255","doi-asserted-by":"crossref","first-page":"1620","DOI":"10.1002\/pro.2158","article-title":"Structural basis for proton conduction and inhibition by the influenza M2 protein","volume":"21","author":"Hong","year":"2012","journal-title":"Protein Sci."},{"key":"10.1016\/j.jmr.2014.08.007_b0260","doi-asserted-by":"crossref","first-page":"11301","DOI":"10.1073\/pnas.94.21.11301","article-title":"A functionally defined model for the M2 proton channel of influenza A virus suggests a mechanism for its ion selectivity","volume":"94","author":"Pinto","year":"1997","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jmr.2014.08.007_b0265","doi-asserted-by":"crossref","first-page":"3703","DOI":"10.1021\/ja2081185","article-title":"NMR detection of pH-dependent histidine-water proton exchange reveals the conduction mechanism of a transmembrane proton channel","volume":"134","author":"Hu","year":"2012","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jmr.2014.08.007_b0270","doi-asserted-by":"crossref","first-page":"9885","DOI":"10.1021\/ja4041412","article-title":"Drug-induced conformational and dynamical changes of the S31N mutant of the influenza M2 proton channel investigated by solid-state NMR","volume":"135","author":"Williams","year":"2013","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jmr.2014.08.007_b0275","doi-asserted-by":"crossref","first-page":"1127","DOI":"10.1016\/j.jmb.2008.11.022","article-title":"Structure of amantadine-bound M2 transmembrane peptide of influenza A in lipid bilayers from magic-angle-spinning solid-state NMR: the role of Ser31 in amantadine binding","volume":"385","author":"Cady","year":"2009","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmr.2014.08.007_b0280","doi-asserted-by":"crossref","first-page":"15075","DOI":"10.1073\/pnas.1007071107","article-title":"Structural mechanism of proton transport through the influenza A M2 protein","volume":"107","author":"Acharya","year":"2010","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jmr.2014.08.007_b0285","doi-asserted-by":"crossref","first-page":"591","DOI":"10.1038\/nature06531","article-title":"Structure and mechanism of the M2 proton channel of influenza A virus","volume":"451","author":"Schnell","year":"2008","journal-title":"Nature"},{"key":"10.1016\/j.jmr.2014.08.007_b0290","doi-asserted-by":"crossref","first-page":"4335","DOI":"10.1529\/biophysj.106.090183","article-title":"Backbone structure of the amantadine-blocked trans-membrane domain M2 proton channel from influenza A virus","volume":"92","author":"Hu","year":"2007","journal-title":"Biophys. J."},{"key":"10.1016\/j.jmr.2014.08.007_b0295","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1126\/science.1101373","article-title":"Molecular architecture of the KvAP voltage-dependent K+ channel in a lipid bilayer","volume":"306","author":"Cuello","year":"2004","journal-title":"Science"},{"key":"10.1016\/j.jmr.2014.08.007_b0300","doi-asserted-by":"crossref","first-page":"8693","DOI":"10.1021\/ja3026328","article-title":"Paramagnetic Cu(II) for probing membrane protein structure and function: inhibition mechanism of the influenza M2 proton channel","volume":"134","author":"Su","year":"2012","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jmr.2014.08.007_b0305","doi-asserted-by":"crossref","first-page":"1698","DOI":"10.1016\/j.bpj.2013.02.054","article-title":"PH-dependent conformation, dynamics, and aromatic interaction ofthegating tryptophan residue of the influenza M2 proton channel fromsolid-state NMR","volume":"104","author":"Williams","year":"2013","journal-title":"Biophys. J."},{"key":"10.1016\/j.jmr.2014.08.007_b0310","doi-asserted-by":"crossref","first-page":"6361","DOI":"10.1021\/bi900716s","article-title":"Immobilization of the influenza A M2 transmembrane peptide in virus envelope-mimetic lipid membranes: a solid-state NMR investigation","volume":"48","author":"Luo","year":"2009","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmr.2014.08.007_b0315","doi-asserted-by":"crossref","first-page":"11572","DOI":"10.1021\/ja202051n","article-title":"Membrane-dependent effects of a cytoplasmic helix on the structure and drug binding of the influenza virus M2 protein","volume":"133","author":"Cady","year":"2011","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jmr.2014.08.007_b0320","doi-asserted-by":"crossref","first-page":"10825","DOI":"10.1021\/jp073823k","article-title":"Sidechain conformation and gating of the M2 transmembrane peptide proton channel of influenza A virus from solid-state NMR","volume":"111","author":"Luo","year":"2007","journal-title":"J. Phys. Chem."}],"container-title":["Journal of Magnetic Resonance"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1090780714002201?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1090780714002201?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2018,9,30]],"date-time":"2018-09-30T05:30:44Z","timestamp":1538285444000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1090780714002201"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2014,10]]},"references-count":64,"alternative-id":["S1090780714002201"],"URL":"https:\/\/doi.org\/10.1016\/j.jmr.2014.08.007","relation":{},"ISSN":["1090-7807"],"issn-type":[{"value":"1090-7807","type":"print"}],"subject":[],"published":{"date-parts":[[2014,10]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Probing membrane protein structure using water polarization transfer solid-state NMR","name":"articletitle","label":"Article Title"},{"value":"Journal of Magnetic Resonance","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jmr.2014.08.007","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2014 Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}]}}