Home > Publications database > Simulation of Top7-CFr: a transient helix extension guides folding > print

001     519
005     20180208233711.0
024 7 _ |2 pmid
|a pmid:18408166
024 7 _ |2 pmc
|a pmc:PMC2786944
024 7 _ |2 DOI
|a 10.1073/pnas.0708411105
024 7 _ |2 WOS
|a WOS:000256781800020
037 _ _ |a PreJuSER-519
041 _ _ |a eng
082 _ _ |a 000
084 _ _ |2 WoS
|a Multidisciplinary Sciences
100 1 _ |a Mohanty, S.
|b 0
|u FZJ
|0 P:(DE-Juel1)132590
245 _ _ |a Simulation of Top7-CFr: a transient helix extension guides folding
260 _ _ |a Washington, DC
|b Academy
|c 2008
300 _ _ |a 8004 - 8007
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 Proceedings of the National Academy of Sciences of the United States of America
|x 0027-8424
|0 5100
|v 105
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a Protein structures often feature beta-sheets in which adjacent beta-strands have large sequence separation. How the folding process orchestrates the formation and correct arrangement of these strands is not comprehensively understood. Particularly challenging are proteins in which beta-strands at the N and C termini are neighbors in a beta-sheet. The N-terminal beta-strand is synthesized early on, but it can not bind to the C terminus before the chain is fully synthesized. During this time, there is a danger that the beta-strand at the N terminus interacts with nearby molecules, leading to potentially harmful aggregates of incompletely folded proteins. Simulations of the C-terminal fragment of Top7 show that this risk of misfolding and aggregation can be avoided by a "caching" mechanism that relies on the "chameleon" behavior of certain segments.
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 Peptide Fragments: chemistry
650 _ 2 |2 MeSH
|a Protein Folding
650 _ 2 |2 MeSH
|a Protein Structure, Secondary
650 _ 2 |2 MeSH
|a Proteins: chemistry
650 _ 2 |2 MeSH
|a Proteins: metabolism
650 _ 2 |2 MeSH
|a Temperature
650 _ 2 |2 MeSH
|a Thermodynamics
650 _ 7 |0 0
|2 NLM Chemicals
|a Peptide Fragments
650 _ 7 |0 0
|2 NLM Chemicals
|a Proteins
650 _ 7 |a J
|2 WoSType
653 2 0 |2 Author
|a protein folding
653 2 0 |2 Author
|a all-atom simulation
653 2 0 |2 Author
|a folding mechanism
653 2 0 |2 Author
|a chameleon segment
653 2 0 |2 Author
|a nonnative intermediates
700 1 _ |a Meinke, J.
|b 1
|u FZJ
|0 P:(DE-Juel1)132189
700 1 _ |a Zimmermann, O.
|b 2
|u FZJ
|0 P:(DE-Juel1)132307
700 1 _ |a Hansmann, U. H. E.
|b 3
|u FZJ
|0 P:(DE-Juel1)VDB46160
773 _ _ |a 10.1073/pnas.0708411105
|g Vol. 105, p. 8004 - 8007
|p 8004 - 8007
|q 105<8004 - 8007
|0 PERI:(DE-600)1461794-8
|t Proceedings of the National Academy of Sciences of the United States of America
|v 105
|y 2008
|x 0027-8424
856 7 _ |2 Pubmed Central
|u http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2786944
909 C O |o oai:juser.fz-juelich.de:519
|p VDB
913 1 _ |k P41
|v Scientific Computing
|l Supercomputing
|b Schlüsseltechnologien
|0 G:(DE-Juel1)FUEK411
|x 0
914 1 _ |y 2008
915 _ _ |0 StatID:(DE-HGF)0010
|a JCR/ISI refereed
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)101081
980 _ _ |a VDB
980 _ _ |a ConvertedRecord
980 _ _ |a journal
980 _ _ |a I:(DE-Juel1)NIC-20090406
980 _ _ |a UNRESTRICTED

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