{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,2]],"date-time":"2026-09-02T00:34:23Z","timestamp":1788309263882,"version":"build-2803163510"},"reference-count":70,"publisher":"Elsevier BV","issue":"35","license":[{"start":{"date-parts":[[2016,8,1]],"date-time":"2016-08-01T00:00:00Z","timestamp":1470009600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,8,22]],"date-time":"2020-08-22T00:00:00Z","timestamp":1598054400000},"content-version":"vor","delay-in-days":1482,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["1R15 GM111681\u201302"],"award-info":[{"award-number":["1R15 GM111681\u201302"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["P20GM103395"],"award-info":[{"award-number":["P20GM103395"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2016,8]]},"DOI":"10.1074\/jbc.m116.740530","type":"journal-article","created":{"date-parts":[[2016,7,12]],"date-time":"2016-07-12T01:07:49Z","timestamp":1468285669000},"page":"18484-18495","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":49,"title":["Flexibility and Solvation of Amyloid-\u03b2 Hydrophobic Core"],"prefix":"10.1016","volume":"291","author":[{"given":"Liliya","family":"Vugmeyster","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Matthew A.","family":"Clark","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Isaac B.","family":"Falconer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dmitry","family":"Ostrovsky","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Donald","family":"Gantz","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wei","family":"Qiang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gina L.","family":"Hoatson","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1074\/jbc.M116.740530_bib1","doi-asserted-by":"crossref","first-page":"7443","DOI":"10.1073\/pnas.0812033106","article-title":"Seeded growth of \u03b2-amyloid fibrils from Alzheimer's brain-derived fibrils produces a distinct fibril structure","volume":"106","author":"Paravastu","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M116.740530_bib2","doi-asserted-by":"crossref","first-page":"1089","DOI":"10.1016\/j.febslet.2012.12.006","article-title":"Breaking the amyloidogenicity code: methods to predict amyloids from amino acid sequence","volume":"587","author":"Ahmed","year":"2013","journal-title":"FEBS Lett"},{"key":"10.1074\/jbc.M116.740530_bib3","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1016\/j.ab.2004.01.014","article-title":"Kinetic analysis of \u03b2-amyloid fibril elongation","volume":"328","author":"Cannon","year":"2004","journal-title":"Anal. Biochem"},{"key":"10.1074\/jbc.M116.740530_bib4","first-page":"195A","article-title":"A missing link in amyloid misfolding: structural insights into amyloid intermediates for Alzheimer's \u03b2-amyloid, A\u03b2(1\u201340) by solid-state NMR","volume":"S","author":"Chimon","year":"2007","journal-title":"Biophys. J"},{"key":"10.1074\/jbc.M116.740530_bib5","doi-asserted-by":"crossref","first-page":"5468","DOI":"10.1073\/pnas.1219476110","article-title":"Atomic structure and hierarchical assembly of a cross-\u03b2 amyloid fibril","volume":"110","author":"Fitzpatrick","year":"2013","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M116.740530_bib6","doi-asserted-by":"crossref","first-page":"697","DOI":"10.1002\/ana.1009","article-title":"Novel amyloid precursor protein mutation in an Iowa family with dementia and severe cerebral amyloid angiopathy","volume":"49","author":"Grabowski","year":"2001","journal-title":"Ann. Neurol"},{"key":"10.1074\/jbc.M116.740530_bib7","doi-asserted-by":"crossref","first-page":"503","DOI":"10.1016\/j.jmb.2010.06.023","article-title":"A\u03b2(1\u201340) forms five distinct amyloid structures whose \u03b2-sheet contents and fibril stabilities are correlated","volume":"401","author":"Kodali","year":"2010","journal-title":"J. Mol. Biol"},{"key":"10.1074\/jbc.M116.740530_bib8","doi-asserted-by":"crossref","first-page":"14686","DOI":"10.1021\/ja203736z","article-title":"Structural complexity of a composite amyloid fibril","volume":"133","author":"Lewandowski","year":"2011","journal-title":"J. Am. Chem. Soc"},{"key":"10.1074\/jbc.M116.740530_bib9","doi-asserted-by":"crossref","first-page":"17342","DOI":"10.1073\/pnas.0506723102","article-title":"3D structure of Alzheimer's amyloid-\u03b2(1\u201342) fibrils","volume":"102","author":"L\u00fchrs","year":"2005","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M116.740530_bib10","doi-asserted-by":"crossref","first-page":"12709","DOI":"10.1021\/bi050927h","article-title":"Thermodynamics of A\u03b2(1\u201340) amyloid fibril elongation","volume":"44","author":"O'Nuallain","year":"2005","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.M116.740530_bib11","doi-asserted-by":"crossref","first-page":"262","DOI":"10.1126\/science.1105850","article-title":"Self-propagating, molecular-level polymorphism in Alzheimer's \u03b2-amyloid fibrils","volume":"307","author":"Petkova","year":"2005","journal-title":"Science"},{"key":"10.1074\/jbc.M116.740530_bib12","doi-asserted-by":"crossref","first-page":"6860","DOI":"10.1021\/ja311963f","article-title":"Polymorph-specific kinetics and thermodynamics of \u03b2 amyloid fibril growth","volume":"135","author":"Qiang","year":"2013","journal-title":"J. Am. Chem. Soc"},{"key":"10.1074\/jbc.M116.740530_bib13","doi-asserted-by":"crossref","first-page":"4443","DOI":"10.1073\/pnas.1111305109","article-title":"Antiparallel \u03b2-sheet architecture in Iowa-mutant \u03b2-amyloid fibrils","volume":"109","author":"Qiang","year":"2012","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M116.740530_bib14","doi-asserted-by":"crossref","first-page":"567","DOI":"10.1021\/ar0681934","article-title":"Amyloid fibrils: common threads in the natural history of proteins","volume":"39","author":"Wetzel","year":"2006","journal-title":"Acc. Chem. Res"},{"key":"10.1074\/jbc.M116.740530_bib15","doi-asserted-by":"crossref","first-page":"11757","DOI":"10.1021\/bi010805z","article-title":"Structural features of the A\u03b2 amyloid fibril elucidated by limited proteolysis","volume":"40","author":"Kheterpal","year":"2001","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.M116.740530_bib16","doi-asserted-by":"crossref","first-page":"454","DOI":"10.1016\/j.jmb.2012.08.004","article-title":"Fiber diffraction data indicate a hollow core for the Alzheimer's A\u03b2 3-fold symmetric fibril","volume":"423","author":"McDonald","year":"2012","journal-title":"J. Mol. Biol"},{"key":"10.1074\/jbc.M116.740530_bib17","doi-asserted-by":"crossref","first-page":"846","DOI":"10.1002\/cbic.201300103","article-title":"A label-free, quantitative assay of amyloid fibril growth based on intrinsic fluorescence","volume":"14","author":"Pinotsi","year":"2013","journal-title":"Chembiochem"},{"key":"10.1074\/jbc.M116.740530_bib18","doi-asserted-by":"crossref","first-page":"6324","DOI":"10.1021\/ja909074j","article-title":"Structural variations in the cross-\u03b2 core of amyloid \u03b2 fibrils revealed by deep UV resonance Raman spectroscopy","volume":"132","author":"Popova","year":"2010","journal-title":"J. Am. Chem. Soc"},{"key":"10.1074\/jbc.M116.740530_bib19","doi-asserted-by":"crossref","first-page":"7462","DOI":"10.1073\/pnas.0712290105","article-title":"Paired \u03b2-sheet structure of an A\u03b2(1\u201340) amyloid fibril revealed by electron microscopy","volume":"105","author":"Sachse","year":"2008","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M116.740530_bib20","doi-asserted-by":"crossref","first-page":"9","DOI":"10.3233\/JAD-122389","article-title":"Modification of amyloid-\u03b2(1\u201342) fibril structure by methionine-35 oxidation","volume":"37","author":"Hou","year":"2013","journal-title":"J. Alzheimers Dis"},{"key":"10.1074\/jbc.M116.740530_bib21","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1002\/anie.201408598","article-title":"Atomic-resolution three-dimensional structure of amyloid \u03b2 fibrils bearing the Osaka mutation","volume":"54","author":"Sch\u00fctz","year":"2015","journal-title":"Angew. Chem. Int. Ed. Engl"},{"key":"10.1074\/jbc.M116.740530_bib22","doi-asserted-by":"crossref","first-page":"216","DOI":"10.1016\/j.str.2014.10.022","article-title":"Modeling an in-register, parallel \u201cIowa\u201d A-\u03b2 fibril structure using solid state NMR data from labeled samples with Rosetta modeling","volume":"23","author":"Sgourakis","year":"2015","journal-title":"Structure"},{"key":"10.1074\/jbc.M116.740530_bib23","doi-asserted-by":"crossref","first-page":"18349","DOI":"10.1073\/pnas.0806270105","article-title":"Molecular structural basis for polymorphism in Alzheimer's \u03b2-amyloid fibrils","volume":"105","author":"Paravastu","year":"2008","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M116.740530_bib24","doi-asserted-by":"crossref","first-page":"498","DOI":"10.1021\/bi051952q","article-title":"Experimental constraints on quaternary structure in Alzheimer's \u03b2-amyloid fibrils","volume":"45","author":"Petkova","year":"2006","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.M116.740530_bib25","doi-asserted-by":"crossref","first-page":"16013","DOI":"10.1021\/ja2035859","article-title":"A new structural model of A\u03b2(40) fibrils","volume":"133","author":"Bertini","year":"2011","journal-title":"J. Am. Chem. Soc"},{"key":"10.1074\/jbc.M116.740530_bib26","doi-asserted-by":"crossref","first-page":"15436","DOI":"10.1021\/bi0204185","article-title":"Supramolecular structural constraints on Alzheimer's \u03b2-amyloid fibrils from electron microscopy and solid-state nuclear magnetic resonance","volume":"41","author":"Antzutkin","year":"2002","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.M116.740530_bib27","doi-asserted-by":"crossref","first-page":"13407","DOI":"10.1073\/pnas.95.23.13407","article-title":"Propagating structure of Alzheimer's \u03b2-amyloid (10\u201335) is parallel \u03b2-sheet with residues in exact register","volume":"95","author":"Benzinger","year":"1998","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M116.740530_bib28","doi-asserted-by":"crossref","first-page":"40810","DOI":"10.1074\/jbc.M205659200","article-title":"Structural and dynamic features of Alzheimer's A\u03b2 peptide in amyloid fibrils studied by site-directed spin labeling","volume":"277","author":"T\u00f6r\u00f6k","year":"2002","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M116.740530_bib29","doi-asserted-by":"crossref","first-page":"4018","DOI":"10.1021\/ja109679q","article-title":"Structural Evolution of Iowa mutant \u03b2-amyloid fibrils from polymorphic to homogeneous states under repeated seeded growth","volume":"133","author":"Qiang","year":"2011","journal-title":"J. Am. Chem. Soc"},{"key":"10.1074\/jbc.M116.740530_bib30","doi-asserted-by":"crossref","first-page":"6072","DOI":"10.1021\/bi9002666","article-title":"Evidence for novel \u03b2-sheet structures in Iowa mutant \u03b2-amyloid fibrils","volume":"48","author":"Tycko","year":"2009","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.M116.740530_bib31","doi-asserted-by":"crossref","first-page":"1781","DOI":"10.1126\/science.1131864","article-title":"Exogenous induction of cerebral \u03b2-amyloidogenesis is governed by agent and host","volume":"313","author":"Meyer-Luehmann","year":"2006","journal-title":"Science"},{"key":"10.1074\/jbc.M116.740530_bib32","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1006\/jsbi.2000.4259","article-title":"Studies on the in vitro assembly of A\u03b2 1\u201340: implications for the search for A\u03b2 fibril formation inhibitors","volume":"130","author":"Goldsbury","year":"2000","journal-title":"J. Struct. Biol"},{"key":"10.1074\/jbc.M116.740530_bib33","doi-asserted-by":"crossref","first-page":"3507","DOI":"10.1007\/s00018-014-1634-z","article-title":"Transient dynamics of A\u03b2 contribute to toxicity in Alzheimer's disease","volume":"71","author":"Hubin","year":"2014","journal-title":"Cell. Mol. Life Sci"},{"key":"10.1074\/jbc.M116.740530_bib34","doi-asserted-by":"crossref","first-page":"1992","DOI":"10.1021\/ja036813f","article-title":"Solution NMR studies of the A\u03b2(1\u201340) and A\u03b2(1\u201342) peptides establish that the met35 oxidation state affects the mechanism of amyloid formation","volume":"126","author":"Hou","year":"2004","journal-title":"J. Am. Chem. Soc"},{"key":"10.1074\/jbc.M116.740530_bib35","doi-asserted-by":"crossref","first-page":"5930","DOI":"10.1046\/j.0014-2956.2001.02537.x","article-title":"NMR studies in aqueous solution fail to identify significant conformational differences between the monomeric forms of two Alzheimer peptides with widely different plaque-competence, A\u03b2(1\u201340)(ox) and A\u03b2(1\u201342)(ox)","volume":"268","author":"Riek","year":"2001","journal-title":"Eur. J. Biochem"},{"key":"10.1074\/jbc.M116.740530_bib36","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1006\/jsbi.2000.4288","article-title":"The Alzheimer's peptide A\u03b2 adopts a collapsed coil structure in water","volume":"130","author":"Zhang","year":"2000","journal-title":"J. Struct. Biol"},{"key":"10.1074\/jbc.M116.740530_bib37","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/s10858-014-9822-6","article-title":"Dynamics in the solid-state: perspectives for the investigation of amyloid aggregates, membrane proteins and soluble protein complexes","volume":"59","author":"Linser","year":"2014","journal-title":"J. Biomol. NMR"},{"key":"10.1074\/jbc.M116.740530_bib38","doi-asserted-by":"crossref","first-page":"1186","DOI":"10.1038\/nprot.2010.72","article-title":"Preparation and characterization of toxic A\u03b2 aggregates for structural and functional studies in Alzheimer's disease research","volume":"5","author":"Jan","year":"2010","journal-title":"Nat. Protoc"},{"key":"10.1074\/jbc.M116.740530_bib39","doi-asserted-by":"crossref","first-page":"717","DOI":"10.1016\/j.jmb.2009.09.039","article-title":"The common architecture of cross-\u03b2 amyloid","volume":"395","author":"Jahn","year":"2010","journal-title":"J. Mol. Biol"},{"key":"10.1074\/jbc.M116.740530_bib40","doi-asserted-by":"crossref","first-page":"833","DOI":"10.1016\/j.jmb.2003.11.008","article-title":"Mapping A\u03b2 amyloid fibril secondary structure using scanning proline mutagenesis","volume":"335","author":"Williams","year":"2004","journal-title":"J. Mol. Biol"},{"key":"10.1074\/jbc.M116.740530_bib41","doi-asserted-by":"crossref","first-page":"2017","DOI":"10.1074\/jbc.M111.308619","article-title":"Dynamics of amyloid \u03b2 fibrils revealed by solid state NMR","volume":"287","author":"Scheidt","year":"2012","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M116.740530_bib42","doi-asserted-by":"crossref","first-page":"477","DOI":"10.1074\/jbc.M508962200","article-title":"The solvent protection of Alzheimer amyloid-\u03b2-(1\u201342) fibrils as determined by solution NMR spectroscopy","volume":"281","author":"Olofsson","year":"2006","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M116.740530_bib43","doi-asserted-by":"crossref","first-page":"4434","DOI":"10.1021\/bi048292u","article-title":"Hydrogen-deuterium (H\/D) exchange mapping of A ss(1\u201340) amyloid fibril secondary structure using nuclear magnetic resonance spectroscopy","volume":"44","author":"Whittemore","year":"2005","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.M116.740530_bib44","doi-asserted-by":"crossref","first-page":"13597","DOI":"10.1073\/pnas.250288897","article-title":"A\u03b2 amyloid fibrils possess a core structure highly resistant to hydrogen exchange","volume":"97","author":"Kheterpal","year":"2000","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M116.740530_bib45","doi-asserted-by":"crossref","first-page":"9507","DOI":"10.1021\/bi0342766","article-title":"Hydrogen exchange-mass spectrometry analysis of \u03b2-amyloid peptide structure","volume":"42","author":"Wang","year":"2003","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.M116.740530_bib46","doi-asserted-by":"crossref","first-page":"785","DOI":"10.1016\/j.jmb.2006.06.066","article-title":"Structural differences in A\u03b2 amyloid protofibrils and fibrils mapped by hydrogen exchange-mass spectrometry with on-line proteolytic fragmentation","volume":"361","author":"Kheterpal","year":"2006","journal-title":"J. Mol. Biol"},{"key":"10.1074\/jbc.M116.740530_bib47","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1038\/nature05695","article-title":"Atomic structures of amyloid cross-\u03b2 spines reveal varied steric zippers","volume":"447","author":"Sawaya","year":"2007","journal-title":"Nature"},{"key":"10.1074\/jbc.M116.740530_bib48","doi-asserted-by":"crossref","first-page":"4653","DOI":"10.1073\/pnas.0901085106","article-title":"Interprotofilament interactions between Alzheimer's A\u03b2(1\u201342) peptides in amyloid fibrils revealed by cryoEM","volume":"106","author":"Zhang","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M116.740530_bib49","doi-asserted-by":"crossref","first-page":"2742","DOI":"10.1021\/ja1100273","article-title":"The unique Alzheimer's \u03b2-amyloid triangular fibril has a cavity along the fibril axis under physiological conditions","volume":"133","author":"Miller","year":"2011","journal-title":"J. Am. Chem. Soc"},{"key":"10.1074\/jbc.M116.740530_bib50","doi-asserted-by":"crossref","first-page":"3046","DOI":"10.1529\/biophysj.107.110700","article-title":"Modeling the Alzheimer A\u03b2(17\u201342) fibril architecture: tight intermolecular sheet-sheet association and intramolecular hydrated cavities","volume":"93","author":"Zheng","year":"2007","journal-title":"Biophys. J"},{"key":"10.1074\/jbc.M116.740530_bib51","doi-asserted-by":"crossref","first-page":"1839","DOI":"10.1021\/acs.biochem.5b01272","article-title":"Sulindac sulfide induces the formation of large oligomeric aggregates of the Alzheimer's disease amyloid-\u03b2 peptide which exhibit reduced neurotoxicity","volume":"55","author":"Prade","year":"2016","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.M116.740530_bib52","doi-asserted-by":"crossref","first-page":"28737","DOI":"10.1074\/jbc.M115.675215","article-title":"Structural mechanism of the interaction of Alzheimer Disease A\u03b2 fibrils with the non-steroidal anti-inflammatory drug (NSAID) sulindac sulfide","volume":"290","author":"Prade","year":"2015","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M116.740530_bib53","doi-asserted-by":"crossref","first-page":"7461","DOI":"10.1039\/C3CP54501F","article-title":"Local interactions influence the fibrillation kinetics, structure and dynamics of A\u03b2(1\u201340) but leave the general fibril structure unchanged","volume":"16","author":"Adler","year":"2014","journal-title":"Phys. Chem. Chem. Phys"},{"key":"10.1074\/jbc.M116.740530_bib54","doi-asserted-by":"crossref","first-page":"10345","DOI":"10.1002\/anie.201405180","article-title":"Characterizing methyl-bearing side chain contacts and dynamics mediating amyloid \u03b2 protofibril interactions using C-13(methyl)-DEST and lifetime line broadening","volume":"53","author":"Fawzi","year":"2014","journal-title":"Angew. Chem. Int. Ed. Engl"},{"key":"10.1074\/jbc.M116.740530_bib55","series-title":"Advances in Magnetic and Optical Resonance","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1016\/B978-0-12-025516-0.50006-1","article-title":"Deuterium relaxation in molecular solids","author":"Vold","year":"1991"},{"key":"10.1074\/jbc.M116.740530_bib56","doi-asserted-by":"crossref","first-page":"10637","DOI":"10.1021\/bi201515b","article-title":"Slow motions in the hydrophobic core of chicken villin headpiece subdomain and their contributions to configurational entropy and heat capacity from solid-state deuteron NMR measurements","volume":"50","author":"Vugmeyster","year":"2011","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.M116.740530_bib57","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1002\/pro.5560050116","article-title":"Dynamics of the three methionyl side chains of Streptomyces subtilisin inhibitor: deuterium NMR studies in solution and in the solid state","volume":"5","author":"Tamura","year":"1996","journal-title":"Protein Sci"},{"key":"10.1074\/jbc.M116.740530_bib58","doi-asserted-by":"crossref","first-page":"10022","DOI":"10.1021\/jp900337x","article-title":"C-13 and N-15 NMR study of the hydration response of T4 lysozyme and \u03b1B-crystallin internal dynamics","volume":"113","author":"Krushelnitsky","year":"2009","journal-title":"J. Phys. Chem. B"},{"key":"10.1074\/jbc.M116.740530_bib59","doi-asserted-by":"crossref","first-page":"238102","DOI":"10.1103\/PhysRevLett.108.238102","article-title":"Surface hydration amplifies single-well protein atom diffusion propagating in the macromolecular core","volume":"108","author":"Hong","year":"2012","journal-title":"Phys. Rev. Lett"},{"key":"10.1074\/jbc.M116.740530_bib60","doi-asserted-by":"crossref","first-page":"386","DOI":"10.1073\/pnas.79.2.386","article-title":"Characterization of leucine side-chain reorientation in collagen fibrils by solid-state H-2 NMR","volume":"79","author":"Batchelder","year":"1982","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M116.740530_bib61","doi-asserted-by":"crossref","first-page":"13288","DOI":"10.1073\/pnas.1003832107","article-title":"Sum frequency generation and solid-state NMR study of the structure, orientation, and dynamics of polystyrene-adsorbed peptides","volume":"107","author":"Weidner","year":"2010","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M116.740530_bib62","doi-asserted-by":"crossref","first-page":"13651","DOI":"10.1021\/ja902977u","article-title":"Probing the dynamics of a protein hydrophobic core by deuteron solid-state nuclear magnetic resonance spectroscopy","volume":"131","author":"Vugmeyster","year":"2009","journal-title":"J. Am. Chem. Soc"},{"key":"10.1074\/jbc.M116.740530_bib63","doi-asserted-by":"crossref","first-page":"423","DOI":"10.1016\/j.str.2010.01.012","article-title":"Dynameomics: a comprehensive database of protein dynamics","volume":"18","author":"van der Kamp","year":"2010","journal-title":"Structure"},{"key":"10.1074\/jbc.M116.740530_bib64","doi-asserted-by":"crossref","first-page":"501","DOI":"10.1038\/35078119","article-title":"Microscopic origins of entropy, heat capacity and the glass transition in proteins","volume":"411","author":"Lee","year":"2001","journal-title":"Nature"},{"key":"10.1074\/jbc.M116.740530_bib65","doi-asserted-by":"crossref","first-page":"562","DOI":"10.1002\/pro.2045","article-title":"Thermal coefficients of the methyl groups within ubiquitin","volume":"21","author":"Sabo","year":"2012","journal-title":"Protein Sci"},{"key":"10.1074\/jbc.M116.740530_bib66","doi-asserted-by":"crossref","first-page":"L43","DOI":"10.1529\/biophysj.106.102160","article-title":"Temperature dependence of fast dynamics in proteins","volume":"92","author":"Song","year":"2007","journal-title":"Biophys. J"},{"key":"10.1074\/jbc.M116.740530_bib67","doi-asserted-by":"crossref","first-page":"1672","DOI":"10.1021\/cr040422h","article-title":"Characterization of the fast dynamics of protein amino acid side chains using NMR relaxation in solution","volume":"106","author":"Igumenova","year":"2006","journal-title":"Chem. Rev"},{"key":"10.1074\/jbc.M116.740530_bib68","doi-asserted-by":"crossref","first-page":"5129","DOI":"10.1073\/pnas.0900336106","article-title":"A unified model of protein dynamics","volume":"106","author":"Frauenfelder","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M116.740530_bib69","series-title":"Electron Microscopy in Biology","first-page":"203","article-title":"Negative staining","author":"Harris","year":"1991"},{"key":"10.1074\/jbc.M116.740530_bib70","series-title":"Advances in Optical and Electron Microscopy","first-page":"107","article-title":"Mounting of macromolecules for electron microscopy with particular reference to surface phenomena and treatment of support films by glow discharge","author":"Dubochet","year":"1982"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820322080?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820322080?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1074\/jbc.M116.740530","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,1,4]],"date-time":"2022-01-04T04:59:04Z","timestamp":1641272344000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925820322080"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2016,8]]},"references-count":70,"journal-issue":{"issue":"35","published-print":{"date-parts":[[2016,8]]}},"alternative-id":["S0021925820322080"],"URL":"https:\/\/doi.org\/10.1074\/jbc.m116.740530","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2016,8]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Flexibility and Solvation of Amyloid-\u03b2 Hydrophobic Core","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1074\/jbc.M116.740530","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2016 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.","name":"copyright","label":"Copyright"}]}}