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000004647 0247_ $$2pmid$$apmid:19191249
000004647 0247_ $$2DOI$$a10.1002/cbic.200800739
000004647 0247_ $$2WOS$$aWOS:000264168000015
000004647 037__ $$aPreJuSER-4647
000004647 041__ $$aeng
000004647 082__ $$a540
000004647 084__ $$2WoS$$aBiochemistry & Molecular Biology
000004647 084__ $$2WoS$$aChemistry, Medicinal
000004647 1001_ $$0P:(DE-Juel1)VDB72840$$aRosenkranz, T.$$b0$$uFZJ
000004647 245__ $$aObserving Proteins as Single Molecules Encapsulated in Surface-Tethered Polymeric Nanocontainers
000004647 260__ $$aWeinheim$$bWiley-VCH$$c2009
000004647 300__ $$a702 - 709
000004647 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000004647 3367_ $$2BibTeX$$aARTICLE
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000004647 3367_ $$2DRIVER$$aarticle
000004647 440_0 $$08962$$aChemBioChem$$v10$$x1439-4227$$y4
000004647 500__ $$aJurgen Groll (SusTech GmbH & Co KG, Darmstadt) is greatly acknowledged for providing us with a protocol for cover slide coatings. We thank Iris v. d. Hocht for providing Atto655-labeled DOPE. T.R. acknowledges financial support by the International Helmholtz Research School on Biophysics and Soft Matter ("Bio-Soft'). J.F thanks G. Buldt (Forschungszentrum Julich) for continuous and sustainable support in his institute.
000004647 520__ $$aImmobilizing biomolecules provides the advantage of observing them individually for extended time periods, which is impossible to accomplish for freely diffusing molecules in solution. In order to immobilize individual protein molecules, we encapsulated them in polymeric vesicles made of amphiphilic triblock copolymers and tethered the vesicles to a cover slide surface. A major goal of this study is to investigate polymeric vesicles with respect to their suitability for protein-folding studies. The fact that polymeric vesicles possess an extreme stability under various chemical conditions is supported by our observation that harsh unfolding conditions do not perturb the structural integrity of the vesicles. Moreover, polymerosomes prove to be permeable to GdnHCl and, thereby, ideally suited for unfolding and refolding studies with encapsulated proteins. We demonstrate this with encapsulated phosphoglycerate kinase, which was fluorescently labeled with Atto655, a dye that exhibits pronounced photoinduced electron transfer (PET) to a nearby tryptophan residue in the native state. Under unfolding conditions, PET was reduced, and we monitored alternating unfolding and refolding conditions for individual encapsulated proteins.
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000004647 588__ $$aDataset connected to Web of Science, Pubmed
000004647 650_2 $$2MeSH$$aFluorescent Dyes: metabolism
000004647 650_2 $$2MeSH$$aFungal Proteins: chemistry
000004647 650_2 $$2MeSH$$aFungal Proteins: metabolism
000004647 650_2 $$2MeSH$$aHydrophobic and Hydrophilic Interactions
000004647 650_2 $$2MeSH$$aImmobilized Proteins: chemistry
000004647 650_2 $$2MeSH$$aImmobilized Proteins: metabolism
000004647 650_2 $$2MeSH$$aLiposomes: chemistry
000004647 650_2 $$2MeSH$$aNanoparticles: chemistry
000004647 650_2 $$2MeSH$$aPhotochemical Processes
000004647 650_2 $$2MeSH$$aPolymers: chemistry
000004647 650_2 $$2MeSH$$aProtein Denaturation
000004647 650_2 $$2MeSH$$aProtein Folding
000004647 650_2 $$2MeSH$$aProtein Renaturation
000004647 650_2 $$2MeSH$$aSaccharomyces cerevisiae
000004647 650_2 $$2MeSH$$aSurface Properties
000004647 650_7 $$00$$2NLM Chemicals$$aFluorescent Dyes
000004647 650_7 $$00$$2NLM Chemicals$$aFungal Proteins
000004647 650_7 $$00$$2NLM Chemicals$$aImmobilized Proteins
000004647 650_7 $$00$$2NLM Chemicals$$aLiposomes
000004647 650_7 $$00$$2NLM Chemicals$$aPolymers
000004647 650_7 $$2WoSType$$aJ
000004647 65320 $$2Author$$afluorescence spectroscopy
000004647 65320 $$2Author$$aphotoinduced electron transfer
000004647 65320 $$2Author$$aprotein encapsulation
000004647 65320 $$2Author$$aprotein folding
000004647 65320 $$2Author$$asingle-molecule studies
000004647 7001_ $$0P:(DE-Juel1)131971$$aKatranidis, A.$$b1$$uFZJ
000004647 7001_ $$0P:(DE-Juel1)VDB86033$$aAtta, D.$$b2$$uFZJ
000004647 7001_ $$0P:(DE-HGF)0$$aEnderlein, J.$$b3
000004647 7001_ $$0P:(DE-HGF)0$$aGregor, I.$$b4
000004647 7001_ $$0P:(DE-HGF)0$$aGrzelakowski, M.$$b5
000004647 7001_ $$0P:(DE-HGF)0$$aRigler, P.$$b6
000004647 7001_ $$0P:(DE-HGF)0$$aMeier, W.$$b7
000004647 7001_ $$0P:(DE-Juel1)131961$$aFitter, J.$$b8$$uFZJ
000004647 773__ $$0PERI:(DE-600)2020469-3$$a10.1002/cbic.200800739$$gVol. 10, p. 702 - 709$$p702 - 709$$q10<702 - 709$$tChemBioChem$$v10$$x1439-4227$$y2009
000004647 8567_ $$uhttp://dx.doi.org/10.1002/cbic.200800739
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