Hauptseite > Publikationsdatenbank > Folding of proteins with diverse folds > print

001     54183
005     20200423204407.0
017 _ _ |a This version is available at the following Publisher URL: http://www.biophysj.org/
024 7 _ |a pmid:16950845
|2 pmid
024 7 _ |a pmc:PMC1630465
|2 pmc
024 7 _ |a 10.1529/biophysj.106.087668
|2 DOI
024 7 _ |a WOS:000241702500003
|2 WOS
024 7 _ |a 2128/2373
|2 Handle
037 _ _ |a PreJuSER-54183
041 _ _ |a eng
082 _ _ |a 570
084 _ _ |2 WoS
|a Biophysics
100 1 _ |a Mohanty, S.
|b 0
|u FZJ
|0 P:(DE-Juel1)132590
245 _ _ |a Folding of proteins with diverse folds
260 _ _ |a New York, NY
|b Rockefeller Univ. Press
|c 2006
300 _ _ |a 3537
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 Biophysical Journal
|x 0006-3495
|0 882
|v 92
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a Using parallel tempering simulations with high statistics, we investigate the folding and thermodynamic properties of three small proteins with distinct native folds: the all-helical 1RIJ, the all-sheet beta3s, and BBA5, which has a mixed helix-sheet fold. In all three cases, simulations with our energy function find the native structures as global minima in free energy at experimentally relevant temperatures. However, the folding process strongly differs for the three molecules, indicating that the folding mechanism is correlated with the form of the native structure.
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 Computer Simulation
650 _ 2 |2 MeSH
|a Models, Chemical
650 _ 2 |2 MeSH
|a Models, Molecular
650 _ 2 |2 MeSH
|a Models, Statistical
650 _ 2 |2 MeSH
|a Protein Conformation
650 _ 2 |2 MeSH
|a Protein Folding
650 _ 2 |2 MeSH
|a Proteins: chemistry
650 _ 2 |2 MeSH
|a Proteins: ultrastructure
650 _ 7 |0 0
|2 NLM Chemicals
|a Proteins
650 _ 7 |a J
|2 WoSType
700 1 _ |a Hansmann, U. H. E.
|b 1
|u FZJ
|0 P:(DE-Juel1)VDB46160
773 _ _ |a 10.1529/biophysj.106.087668
|g Vol. 91, p. 3537
|p 3537
|q 91<3537
|0 PERI:(DE-600)1477214-0
|t Biophysical journal
|v 91
|y 2006
|x 0006-3495
856 7 _ |2 Pubmed Central
|u http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1630465
856 4 _ |u https://juser.fz-juelich.de/record/54183/files/84949.pdf
|y OpenAccess
856 4 _ |u https://juser.fz-juelich.de/record/54183/files/84949.jpg?subformat=icon-1440
|x icon-1440
|y OpenAccess
856 4 _ |u https://juser.fz-juelich.de/record/54183/files/84949.jpg?subformat=icon-180
|x icon-180
|y OpenAccess
856 4 _ |u https://juser.fz-juelich.de/record/54183/files/84949.jpg?subformat=icon-640
|x icon-640
|y OpenAccess
909 C O |o oai:juser.fz-juelich.de:54183
|p openaire
|p open_access
|p driver
|p VDB
|p dnbdelivery
913 1 _ |k P41
|v Scientific Computing
|l Supercomputing
|b Schlüsseltechnologien
|0 G:(DE-Juel1)FUEK411
|x 0
914 1 _ |y 2006
915 _ _ |0 StatID:(DE-HGF)0010
|a JCR/ISI refereed
915 _ _ |2 StatID
|0 StatID:(DE-HGF)0510
|a OpenAccess
920 1 _ |k NIC
|l John von Neumann - Institut für Computing
|g NIC
|0 I:(DE-Juel1)NIC-20090406
|x 0
970 _ _ |a VDB:(DE-Juel1)84949
980 _ _ |a VDB
980 _ _ |a JUWEL
980 _ _ |a ConvertedRecord
980 _ _ |a journal
980 _ _ |a I:(DE-Juel1)NIC-20090406
980 _ _ |a UNRESTRICTED
980 _ _ |a FullTexts
980 1 _ |a FullTexts

LibraryCollectionCLSMajorCLSMinorLanguageAuthor
Marc 21