000055426 001__ 55426 000055426 005__ 20200423204423.0 000055426 0247_ $$2pmid$$apmid:17212510 000055426 0247_ $$2DOI$$a10.1063/1.2423013 000055426 0247_ $$2WOS$$aWOS:000243380000031 000055426 0247_ $$2Handle$$a2128/19093 000055426 037__ $$aPreJuSER-55426 000055426 041__ $$aeng 000055426 082__ $$a540 000055426 084__ $$2WoS$$aPhysics, Atomic, Molecular & Chemical 000055426 1001_ $$0P:(DE-Juel1)132189$$aMeinke, J.$$b0$$uFZJ 000055426 245__ $$aAggregation of Beta-Amyloid Fragments 000055426 260__ $$aMelville, NY$$bAmerican Institute of Physics$$c2007 000055426 300__ $$a014706 000055426 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article 000055426 3367_ $$2DataCite$$aOutput Types/Journal article 000055426 3367_ $$00$$2EndNote$$aJournal Article 000055426 3367_ $$2BibTeX$$aARTICLE 000055426 3367_ $$2ORCID$$aJOURNAL_ARTICLE 000055426 3367_ $$2DRIVER$$aarticle 000055426 440_0 $$03145$$aJournal of Chemical Physics$$v126$$x0021-9606$$y1 000055426 500__ $$aRecord converted from VDB: 12.11.2012 000055426 520__ $$aThe authors study the folding and aggregation of six chains of the beta-amyloid fragment 16-22 using Monte Carlo simulations. While the isolated fragment prefers a helical form at room temperature, in the system of six interacting fragments one observes both parallel and antiparallel beta sheets below a crossover temperature T(x) approximately equal to 420 K. The antiparallel sheets have lower energy and are therefore more stable. Above the nucleation temperature the aggregate quickly dissolves into widely separated, weakly interacting chains. 000055426 536__ $$0G:(DE-Juel1)FUEK411$$2G:(DE-HGF)$$aScientific Computing$$cP41$$x0 000055426 588__ $$aDataset connected to Web of Science, Pubmed 000055426 650_2 $$2MeSH$$aAmyloid beta-Peptides: chemistry 000055426 650_2 $$2MeSH$$aAmyloid beta-Peptides: ultrastructure 000055426 650_2 $$2MeSH$$aBinding Sites 000055426 650_2 $$2MeSH$$aComputer Simulation 000055426 650_2 $$2MeSH$$aDimerization 000055426 650_2 $$2MeSH$$aModels, Chemical 000055426 650_2 $$2MeSH$$aModels, Molecular 000055426 650_2 $$2MeSH$$aMonte Carlo Method 000055426 650_2 $$2MeSH$$aMultiprotein Complexes: chemistry 000055426 650_2 $$2MeSH$$aMultiprotein Complexes: ultrastructure 000055426 650_2 $$2MeSH$$aPeptide Fragments: chemistry 000055426 650_2 $$2MeSH$$aPeptide Fragments: ultrastructure 000055426 650_2 $$2MeSH$$aProtein Binding 000055426 650_2 $$2MeSH$$aProtein Conformation 000055426 650_2 $$2MeSH$$aProtein Folding 000055426 650_2 $$2MeSH$$aTemperature 000055426 650_7 $$00$$2NLM Chemicals$$aAmyloid beta-Peptides 000055426 650_7 $$00$$2NLM Chemicals$$aMultiprotein Complexes 000055426 650_7 $$00$$2NLM Chemicals$$aPeptide Fragments 000055426 650_7 $$00$$2NLM Chemicals$$aamyloid beta-protein (16-22) 000055426 650_7 $$2WoSType$$aJ 000055426 7001_ $$0P:(DE-Juel1)VDB64885$$aHansmann, U.$$b1$$uFZJ 000055426 773__ $$0PERI:(DE-600)1473050-9$$a10.1063/1.2423013$$gVol. 126, p. 014706$$p014706$$q126<014706$$tThe @journal of chemical physics$$v126$$x0021-9606$$y2007 000055426 8567_ $$uhttp://dx.doi.org/10.1063/1.2423013 000055426 8564_ $$uhttps://juser.fz-juelich.de/record/55426/files/1.2423013.pdf$$yOpenAccess 000055426 8564_ $$uhttps://juser.fz-juelich.de/record/55426/files/1.2423013.gif?subformat=icon$$xicon$$yOpenAccess 000055426 8564_ $$uhttps://juser.fz-juelich.de/record/55426/files/1.2423013.jpg?subformat=icon-180$$xicon-180$$yOpenAccess 000055426 8564_ $$uhttps://juser.fz-juelich.de/record/55426/files/1.2423013.jpg?subformat=icon-700$$xicon-700$$yOpenAccess 000055426 8564_ $$uhttps://juser.fz-juelich.de/record/55426/files/1.2423013.pdf?subformat=pdfa$$xpdfa$$yOpenAccess 000055426 909CO $$ooai:juser.fz-juelich.de:55426$$pdnbdelivery$$pdriver$$pVDB$$popen_access$$popenaire 000055426 9131_ $$0G:(DE-Juel1)FUEK411$$bSchlüsseltechnologien$$kP41$$lSupercomputing$$vScientific Computing$$x0 000055426 9141_ $$y2007 000055426 915__ $$0StatID:(DE-HGF)0510$$2StatID$$aOpenAccess 000055426 915__ $$0StatID:(DE-HGF)0010$$aJCR/ISI refereed 000055426 9201_ $$0I:(DE-Juel1)NIC-20090406$$gNIC$$kNIC$$lJohn von Neumann - Institut für Computing$$x0 000055426 970__ $$aVDB:(DE-Juel1)86441 000055426 980__ $$aVDB 000055426 980__ $$aConvertedRecord 000055426 980__ $$ajournal 000055426 980__ $$aI:(DE-Juel1)NIC-20090406 000055426 980__ $$aUNRESTRICTED 000055426 9801_ $$aFullTexts