000000519 001__ 519
000000519 005__ 20180208233711.0
000000519 0247_ $$2pmid$$apmid:18408166
000000519 0247_ $$2pmc$$apmc:PMC2786944
000000519 0247_ $$2DOI$$a10.1073/pnas.0708411105
000000519 0247_ $$2WOS$$aWOS:000256781800020
000000519 037__ $$aPreJuSER-519
000000519 041__ $$aeng
000000519 082__ $$a000
000000519 084__ $$2WoS$$aMultidisciplinary Sciences
000000519 1001_ $$0P:(DE-Juel1)132590$$aMohanty, S.$$b0$$uFZJ
000000519 245__ $$aSimulation of Top7-CFr: a transient helix extension guides folding
000000519 260__ $$aWashington, DC$$bAcademy$$c2008
000000519 300__ $$a8004 - 8007
000000519 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
000000519 3367_ $$2DataCite$$aOutput Types/Journal article
000000519 3367_ $$00$$2EndNote$$aJournal Article
000000519 3367_ $$2BibTeX$$aARTICLE
000000519 3367_ $$2ORCID$$aJOURNAL_ARTICLE
000000519 3367_ $$2DRIVER$$aarticle
000000519 440_0 $$05100$$aProceedings of the National Academy of Sciences of the United States of America$$v105$$x0027-8424
000000519 500__ $$aRecord converted from VDB: 12.11.2012
000000519 520__ $$aProtein 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.
000000519 536__ $$0G:(DE-Juel1)FUEK411$$2G:(DE-HGF)$$aScientific Computing$$cP41$$x0
000000519 588__ $$aDataset connected to Web of Science, Pubmed
000000519 65320 $$2Author$$aprotein folding
000000519 65320 $$2Author$$aall-atom simulation
000000519 65320 $$2Author$$afolding mechanism
000000519 65320 $$2Author$$achameleon segment
000000519 65320 $$2Author$$anonnative intermediates
000000519 650_2 $$2MeSH$$aComputer Simulation
000000519 650_2 $$2MeSH$$aPeptide Fragments: chemistry
000000519 650_2 $$2MeSH$$aProtein Folding
000000519 650_2 $$2MeSH$$aProtein Structure, Secondary
000000519 650_2 $$2MeSH$$aProteins: chemistry
000000519 650_2 $$2MeSH$$aProteins: metabolism
000000519 650_2 $$2MeSH$$aTemperature
000000519 650_2 $$2MeSH$$aThermodynamics
000000519 650_7 $$00$$2NLM Chemicals$$aPeptide Fragments
000000519 650_7 $$00$$2NLM Chemicals$$aProteins
000000519 650_7 $$2WoSType$$aJ
000000519 7001_ $$0P:(DE-Juel1)132189$$aMeinke, J.$$b1$$uFZJ
000000519 7001_ $$0P:(DE-Juel1)132307$$aZimmermann, O.$$b2$$uFZJ
000000519 7001_ $$0P:(DE-Juel1)VDB46160$$aHansmann, U. H. E.$$b3$$uFZJ
000000519 773__ $$0PERI:(DE-600)1461794-8$$a10.1073/pnas.0708411105$$gVol. 105, p. 8004 - 8007$$p8004 - 8007$$q105<8004 - 8007$$tProceedings of the National Academy of Sciences of the United States of America$$v105$$x0027-8424$$y2008
000000519 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC2786944
000000519 909CO $$ooai:juser.fz-juelich.de:519$$pVDB
000000519 915__ $$0StatID:(DE-HGF)0010$$aJCR/ISI refereed
000000519 9141_ $$y2008
000000519 9131_ $$0G:(DE-Juel1)FUEK411$$bSchlüsseltechnologien$$kP41$$lSupercomputing$$vScientific Computing$$x0
000000519 9201_ $$0I:(DE-Juel1)NIC-20090406$$gNIC$$kNIC$$lJohn von Neumann - Institut für Computing$$x0
000000519 970__ $$aVDB:(DE-Juel1)101081
000000519 980__ $$aVDB
000000519 980__ $$aConvertedRecord
000000519 980__ $$ajournal
000000519 980__ $$aI:(DE-Juel1)NIC-20090406
000000519 980__ $$aUNRESTRICTED