{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,13]],"date-time":"2026-02-13T17:05:11Z","timestamp":1771002311800,"version":"3.50.1"},"reference-count":32,"publisher":"Elsevier BV","issue":"1","license":[{"start":{"date-parts":[[2001,1,1]],"date-time":"2001-01-01T00:00:00Z","timestamp":978307200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2013,7,16]],"date-time":"2013-07-16T00:00:00Z","timestamp":1373932800000},"content-version":"vor","delay-in-days":4579,"URL":"https:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biophysical Journal"],"published-print":{"date-parts":[[2001,1]]},"DOI":"10.1016\/s0006-3495(01)75993-0","type":"journal-article","created":{"date-parts":[[2009,1,6]],"date-time":"2009-01-06T12:50:00Z","timestamp":1231246200000},"page":"31-44","source":"Crossref","is-referenced-by-count":108,"title":["Simulation Study of the Structure and Dynamics of the Alzheimer\u2019s Amyloid Peptide Congener in Solution"],"prefix":"10.1016","volume":"80","author":[{"given":"Francesca","family":"Massi","sequence":"first","affiliation":[]},{"given":"Jeff W.","family":"Peng","sequence":"additional","affiliation":[]},{"given":"Jonathan P.","family":"Lee","sequence":"additional","affiliation":[]},{"given":"John E.","family":"Straub","sequence":"additional","affiliation":[]}],"member":"78","reference":[{"key":"10.1016\/S0006-3495(01)75993-0_bib1","doi-asserted-by":"crossref","first-page":"1075","DOI":"10.1016\/0022-2836(92)90106-T","article-title":"Solution conformations and aggregational properties of synthetic amyloid \u03b2-peptides of Alzheimer\u2019s-disease: analysis of circular-dichroism spectra","volume":"225","author":"Barrow","year":"1992","journal-title":"J. Mol. Biol."},{"key":"10.1016\/S0006-3495(01)75993-0_bib2","series-title":"Dynamic Light Scattering","author":"Berne","year":"1976"},{"key":"10.1016\/S0006-3495(01)75993-0_bib3","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1002\/jcc.540040211","article-title":"Charmm: a program for macromolecular energy minimization and dynamics calculations","volume":"4","author":"Brooks","year":"1983","journal-title":"J. Comp. Chem."},{"key":"10.1016\/S0006-3495(01)75993-0_bib4","series-title":"Protein nmr spectroscopy: Principles and practice","author":"Cavanagh","year":"1996"},{"key":"10.1016\/S0006-3495(01)75993-0_bib5","doi-asserted-by":"crossref","first-page":"174","DOI":"10.1006\/jsbi.2000.4276","article-title":"Activation barriers to structural transition determine deposition rates of Alzheimer\u2019s disease A\u03b2 amyloid","volume":"130","author":"Esler","year":"2000","journal-title":"J. Struct. Biol."},{"key":"10.1016\/S0006-3495(01)75993-0_bib6","doi-asserted-by":"crossref","first-page":"749","DOI":"10.1021\/bi951685w","article-title":"In vitro growth of Alzheimer\u2019s disease beta-amyloid plaques displays first-order kinetics","volume":"35","author":"Esler","year":"1996","journal-title":"Biochemistry"},{"key":"10.1016\/S0006-3495(01)75993-0_bib7","doi-asserted-by":"crossref","first-page":"13914","DOI":"10.1021\/bi961302+","article-title":"Point substitution in the central hydrophobic cluster of a human \u03b2-amyloid congener disrupts peptide folding and abolishes plaque competence","volume":"35","author":"Esler","year":"1996","journal-title":"Biochemistry"},{"key":"10.1016\/S0006-3495(01)75993-0_bib8","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1016\/S1074-5521(97)90255-6","article-title":"Observation of metastable A\u03b2 amyloid protofibrils by atomic force microscopy","volume":"4","author":"Harper","year":"1997","journal-title":"Chem. Biol."},{"key":"10.1016\/S0006-3495(01)75993-0_bib9","doi-asserted-by":"crossref","first-page":"951","DOI":"10.1016\/S1074-5521(97)90303-3","article-title":"Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer\u2019s disease amyloid-\u03b2 protein","volume":"4","author":"Harper","year":"1997","journal-title":"Chem. Biol."},{"key":"10.1016\/S0006-3495(01)75993-0_bib10","doi-asserted-by":"crossref","first-page":"12277","DOI":"10.1073\/pnas.95.21.12277","article-title":"Temperature dependence of amyloid \u03b2-protein fibrillization","volume":"95","author":"Kusumoto","year":"1998","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S0006-3495(01)75993-0_bib11","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1021\/ar950159u","article-title":"A reductionist view of Alzheimer\u2019s disease","volume":"29","author":"Lansbury","year":"1996","journal-title":"Acc. Chem. Res."},{"key":"10.1016\/S0006-3495(01)75993-0_bib12","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1016\/0022-2836(71)90324-X","article-title":"Interpretation of protein structures: Estimation of static accessibility","volume":"55","author":"Lee","year":"1971","journal-title":"J. Mol. Biol."},{"key":"10.1016\/S0006-3495(01)75993-0_bib13","doi-asserted-by":"crossref","first-page":"5191","DOI":"10.1021\/bi00015a033","article-title":"1H NMR of A\u03b2 amyloid peptide congeners in water solution. Conformational changes correlate with plaque competence","volume":"34","author":"Lee","year":"1995","journal-title":"Biochemistry"},{"key":"10.1016\/S0006-3495(01)75993-0_bib14","doi-asserted-by":"crossref","first-page":"4546","DOI":"10.1021\/ja00381a009","article-title":"Model free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules: 1. Theory and range of validity","volume":"104","author":"Lipari","year":"1982","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/S0006-3495(01)75993-0_bib15","doi-asserted-by":"crossref","first-page":"4559","DOI":"10.1021\/ja00381a010","article-title":"Model free approach to the interpretation of Nuclear Magnetic Resonance relaxation in macromolecules: 1. Analysis of experimental results","volume":"104","author":"Lipari","year":"1982","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/S0006-3495(01)75993-0_bib16","doi-asserted-by":"crossref","first-page":"1125","DOI":"10.1073\/pnas.93.3.1125","article-title":"On the nucleation and growth of amyloid \u03b2-protein fibrils: Detection of nuclei and quantitation of rate constants","volume":"93","author":"Lomakin","year":"1996","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S0006-3495(01)75993-0_bib17","doi-asserted-by":"crossref","first-page":"7942","DOI":"10.1073\/pnas.94.15.7942","article-title":"Kinetic theory of fibrillogenesis of amyloid \u03b2-protein","volume":"94","author":"Lomakin","year":"1997","journal-title":"Proc. Natl. Acad. Sci. USA."},{"key":"10.1016\/S0006-3495(01)75993-0_bib18","doi-asserted-by":"crossref","first-page":"3586","DOI":"10.1021\/jp973084f","article-title":"All-atom empirical potential for molecular modeling and dynamics studies of proteins","volume":"102","author":"Mackerell","year":"1998","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/S0006-3495(01)75993-0_bib19","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1111\/j.1750-3639.1996.tb00797.x","article-title":"Brain amyloid: a physicochemical perspective","volume":"6","author":"Maggio","year":"1996","journal-title":"Brain Pathol."},{"key":"10.1016\/S0006-3495(01)75993-0_bib20","doi-asserted-by":"crossref","first-page":"8571","DOI":"10.1021\/bi00151a027","article-title":"Mapping of the spectral densities of the N-H bond motions in eglin c using heteronuclear relaxation experiments","volume":"31","author":"Peng","year":"1992","journal-title":"Biochemistry"},{"key":"10.1016\/S0006-3495(01)75993-0_bib21","doi-asserted-by":"crossref","first-page":"16733","DOI":"10.1021\/bi00051a023","article-title":"Frequency spectrum of NH bonds in eglin c from spectral density mapping at multiple fields","volume":"34","author":"Peng","year":"1995","journal-title":"Biochemistry"},{"key":"10.1016\/S0006-3495(01)75993-0_bib22","doi-asserted-by":"crossref","first-page":"8264","DOI":"10.1021\/j100085a002","article-title":"Internal motions in the molecular tumbling regime: effect on NMR dipolar cross relaxation and interproton distance determination","volume":"98","author":"Philippopoulos","year":"1994","journal-title":"J. Phys. Chem."},{"key":"10.1016\/S0006-3495(01)75993-0_bib23","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1016\/S0959-440X(99)00049-4","article-title":"Amyloid fibrillogenesis: themes and variations","volume":"10","author":"Rochet","year":"2000","journal-title":"Curr. Opin. Struc. Biol."},{"key":"10.1016\/S0006-3495(01)75993-0_bib24","doi-asserted-by":"crossref","first-page":"438","DOI":"10.1097\/00005072-199409000-00003","article-title":"Alzheimer\u2019s disease: a central role for amyloid","volume":"53","author":"Selkoe","year":"1991","journal-title":"J. Neuropath. Exp. Neurol."},{"key":"10.1016\/S0006-3495(01)75993-0_bib25","series-title":"Modelling of Biomolecular Structure and Mechanisms","first-page":"241","article-title":"A program for visualization of structure and dynamics of biomolecules and STO: a program for computing stochastic paths","author":"Simmerling","year":"1995"},{"key":"10.1016\/S0006-3495(01)75993-0_bib26","doi-asserted-by":"crossref","first-page":"121","DOI":"10.3109\/13506129808995290","article-title":"Structural and kinetic features of amyloid \u03b2-protein fibrillogenesis","volume":"5","author":"Teplow","year":"1998","journal-title":"Amyloid: Int. J. Exp. Clin. Invest."},{"key":"10.1016\/S0006-3495(01)75993-0_bib27","doi-asserted-by":"crossref","first-page":"10424","DOI":"10.1021\/bi990718v","article-title":"Deposition of monomeric, not oligomeric, A\u03b2 mediates growth of Alzheimer\u2019s disease amyloid plaques in human brain preparations","volume":"38","author":"Tseng","year":"1999","journal-title":"Biochemistry"},{"key":"10.1016\/S0006-3495(01)75993-0_bib28","doi-asserted-by":"crossref","first-page":"22364","DOI":"10.1074\/jbc.272.35.22364","article-title":"Amyloid \u03b2-protein fibrillogenesis: Detection of a protofibrillar intermediate","volume":"272","author":"Walsh","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0006-3495(01)75993-0_bib29","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1002\/pro.5560010204","article-title":"Atomic solvation parameters applied to molecular dynamics of proteins in solution","volume":"1","author":"Wesson","year":"1992","journal-title":"Protein Sci."},{"key":"10.1016\/S0006-3495(01)75993-0_bib30","unstructured":"Zhang, S. 1999. Studies of b amyloid congeners directed toward understanding the molecular mechanism underlying the formation of amyloid deposits in Alzheimer\u2019s disease. Ph.D. Thesis, Boston University, Boston, MA. 187 pp."},{"key":"10.1016\/S0006-3495(01)75993-0_bib31","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1006\/jsbi.2000.4288","article-title":"The Alzheimer\u2019s peptide A\u03b2 adopts a collapsed coil structure in water","volume":"130","author":"Zhang","year":"2000","journal-title":"J. Struct. Biol."},{"key":"10.1016\/S0006-3495(01)75993-0_bib32","doi-asserted-by":"crossref","first-page":"413","DOI":"10.1016\/S1359-0278(98)00054-6","article-title":"Residual structure in the Alzheimer\u2019s disease peptide: probing the origin of a central hydrophobic cluster","volume":"3","author":"Zhang","year":"1998","journal-title":"Fold. Des."}],"container-title":["Biophysical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006349501759930?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006349501759930?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2018,12,23]],"date-time":"2018-12-23T01:28:56Z","timestamp":1545528536000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0006349501759930"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2001,1]]},"references-count":32,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2001,1]]}},"alternative-id":["S0006349501759930"],"URL":"https:\/\/doi.org\/10.1016\/s0006-3495(01)75993-0","relation":{},"ISSN":["0006-3495"],"issn-type":[{"value":"0006-3495","type":"print"}],"subject":[],"published":{"date-parts":[[2001,1]]}}}