Hauptseite > Publikationsdatenbank > Aggregation of Beta-Amyloid Fragments > print

001     55426
005     20200423204423.0
024 7 _ |a pmid:17212510
|2 pmid
024 7 _ |a 10.1063/1.2423013
|2 DOI
024 7 _ |a WOS:000243380000031
|2 WOS
024 7 _ |a 2128/19093
|2 Handle
037 _ _ |a PreJuSER-55426
041 _ _ |a eng
082 _ _ |a 540
084 _ _ |2 WoS
|a Physics, Atomic, Molecular & Chemical
100 1 _ |a Meinke, J.
|b 0
|u FZJ
|0 P:(DE-Juel1)132189
245 _ _ |a Aggregation of Beta-Amyloid Fragments
260 _ _ |a Melville, NY
|b American Institute of Physics
|c 2007
300 _ _ |a 014706
336 7 _ |a Journal Article
|0 PUB:(DE-HGF)16
|2 PUB:(DE-HGF)
336 7 _ |a Output Types/Journal article
|2 DataCite
336 7 _ |a Journal Article
|0 0
|2 EndNote
336 7 _ |a ARTICLE
|2 BibTeX
336 7 _ |a JOURNAL_ARTICLE
|2 ORCID
336 7 _ |a article
|2 DRIVER
440 _ 0 |a Journal of Chemical Physics
|x 0021-9606
|0 3145
|y 1
|v 126
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a The 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.
536 _ _ |a Scientific Computing
|c P41
|2 G:(DE-HGF)
|0 G:(DE-Juel1)FUEK411
|x 0
588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Amyloid beta-Peptides: chemistry
650 _ 2 |2 MeSH
|a Amyloid beta-Peptides: ultrastructure
650 _ 2 |2 MeSH
|a Binding Sites
650 _ 2 |2 MeSH
|a Computer Simulation
650 _ 2 |2 MeSH
|a Dimerization
650 _ 2 |2 MeSH
|a Models, Chemical
650 _ 2 |2 MeSH
|a Models, Molecular
650 _ 2 |2 MeSH
|a Monte Carlo Method
650 _ 2 |2 MeSH
|a Multiprotein Complexes: chemistry
650 _ 2 |2 MeSH
|a Multiprotein Complexes: ultrastructure
650 _ 2 |2 MeSH
|a Peptide Fragments: chemistry
650 _ 2 |2 MeSH
|a Peptide Fragments: ultrastructure
650 _ 2 |2 MeSH
|a Protein Binding
650 _ 2 |2 MeSH
|a Protein Conformation
650 _ 2 |2 MeSH
|a Protein Folding
650 _ 2 |2 MeSH
|a Temperature
650 _ 7 |0 0
|2 NLM Chemicals
|a Amyloid beta-Peptides
650 _ 7 |0 0
|2 NLM Chemicals
|a Multiprotein Complexes
650 _ 7 |0 0
|2 NLM Chemicals
|a Peptide Fragments
650 _ 7 |0 0
|2 NLM Chemicals
|a amyloid beta-protein (16-22)
650 _ 7 |a J
|2 WoSType
700 1 _ |a Hansmann, U.
|b 1
|u FZJ
|0 P:(DE-Juel1)VDB64885
773 _ _ |a 10.1063/1.2423013
|g Vol. 126, p. 014706
|p 014706
|q 126<014706
|0 PERI:(DE-600)1473050-9
|t The @journal of chemical physics
|v 126
|y 2007
|x 0021-9606
856 7 _ |u http://dx.doi.org/10.1063/1.2423013
856 4 _ |u https://juser.fz-juelich.de/record/55426/files/1.2423013.pdf
|y OpenAccess
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|y OpenAccess
909 C O |o oai:juser.fz-juelich.de:55426
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913 1 _ |k P41
|v Scientific Computing
|l Supercomputing
|b Schlüsseltechnologien
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914 1 _ |y 2007
915 _ _ |a OpenAccess
|0 StatID:(DE-HGF)0510
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915 _ _ |a JCR/ISI refereed
|0 StatID:(DE-HGF)0010
920 1 _ |k NIC
|l John von Neumann - Institut für Computing
|g NIC
|0 I:(DE-Juel1)NIC-20090406
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980 _ _ |a journal
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980 _ _ |a UNRESTRICTED
980 1 _ |a FullTexts

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