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000054183 0247_ $$2pmid$$apmid:16950845
000054183 0247_ $$2pmc$$apmc:PMC1630465
000054183 0247_ $$2DOI$$a10.1529/biophysj.106.087668
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000054183 041__ $$aeng
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000054183 084__ $$2WoS$$aBiophysics
000054183 1001_ $$0P:(DE-Juel1)132590$$aMohanty, S.$$b0$$uFZJ
000054183 245__ $$aFolding of proteins with diverse folds
000054183 260__ $$aNew York, NY$$bRockefeller Univ. Press$$c2006
000054183 300__ $$a3537
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000054183 440_0 $$0882$$aBiophysical Journal$$v92$$x0006-3495
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000054183 520__ $$aUsing parallel tempering simulations with high statistics, we investigate the folding and thermodynamic properties of three small proteins with distinct native folds: the all-helical 1RIJ, the all-sheet beta3s, and BBA5, which has a mixed helix-sheet fold. In all three cases, simulations with our energy function find the native structures as global minima in free energy at experimentally relevant temperatures. However, the folding process strongly differs for the three molecules, indicating that the folding mechanism is correlated with the form of the native structure.
000054183 536__ $$0G:(DE-Juel1)FUEK411$$2G:(DE-HGF)$$aScientific Computing$$cP41$$x0
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000054183 650_2 $$2MeSH$$aComputer Simulation
000054183 650_2 $$2MeSH$$aModels, Chemical
000054183 650_2 $$2MeSH$$aModels, Molecular
000054183 650_2 $$2MeSH$$aModels, Statistical
000054183 650_2 $$2MeSH$$aProtein Conformation
000054183 650_2 $$2MeSH$$aProtein Folding
000054183 650_2 $$2MeSH$$aProteins: chemistry
000054183 650_2 $$2MeSH$$aProteins: ultrastructure
000054183 650_7 $$00$$2NLM Chemicals$$aProteins
000054183 650_7 $$2WoSType$$aJ
000054183 7001_ $$0P:(DE-Juel1)VDB46160$$aHansmann, U. H. E.$$b1$$uFZJ
000054183 773__ $$0PERI:(DE-600)1477214-0$$a10.1529/biophysj.106.087668$$gVol. 91, p. 3537$$p3537$$q91<3537$$tBiophysical journal$$v91$$x0006-3495$$y2006
000054183 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC1630465
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000054183 9131_ $$0G:(DE-Juel1)FUEK411$$bSchlüsseltechnologien$$kP41$$lSupercomputing$$vScientific Computing$$x0
000054183 9141_ $$y2006
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000054183 9201_ $$0I:(DE-Juel1)NIC-20090406$$gNIC$$kNIC$$lJohn von Neumann - Institut für Computing$$x0
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