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000004685 0247_ $$2DOI$$a10.1007/s00018-009-8771-9
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000004685 041__ $$aeng
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000004685 084__ $$2WoS$$aBiochemistry & Molecular Biology
000004685 084__ $$2WoS$$aCell Biology
000004685 1001_ $$0P:(DE-Juel1)131961$$aFitter, J.$$b0$$uFZJ
000004685 245__ $$aThe perspective of studying multi-domain protein folding
000004685 260__ $$aBasel$$bBirkhäuser$$c2009
000004685 300__ $$a1672 - 1681
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000004685 440_0 $$01153$$aCellular and Molecular Life Sciences$$v66$$x1420-682X
000004685 500__ $$aRecord converted from VDB: 12.11.2012
000004685 520__ $$aMost of fundamental studies on protein folding have been performed with small globular proteins consisting of a single domain. In vitro many of these proteins are well characterized by a reversible two-state folding scheme. However, the majority of proteins in the cell belong to the class of larger multi-domain proteins that often unfold irreversibly under in vitro conditions. This makes folding studies difficult or even impossible. In spite of these problems for many multi-domain proteins, folding has been investigated by classical refolding. Co-translational folding of nascent polypeptide chains when synthesized by ribosomes has also been studied. Single molecule techniques represent a promising approach for future studies on the folding of multi-domain proteins, and tremendous advances have been made in these techniques in recent years. In particular, fluorescence-based methods can contribute significantly to an understanding of the fundamental principles of multi-domain protein folding.
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000004685 588__ $$aDataset connected to Web of Science, Pubmed
000004685 650_2 $$2MeSH$$aAnimals
000004685 650_2 $$2MeSH$$aHumans
000004685 650_2 $$2MeSH$$aModels, Molecular
000004685 650_2 $$2MeSH$$aProtein Folding
000004685 650_2 $$2MeSH$$aProtein Structure, Tertiary
000004685 650_2 $$2MeSH$$aProteins: chemistry
000004685 650_2 $$2MeSH$$aSpectrometry, Fluorescence
000004685 650_7 $$00$$2NLM Chemicals$$aProteins
000004685 650_7 $$2WoSType$$aJ
000004685 65320 $$2Author$$aIrreversible unfolding
000004685 65320 $$2Author$$aprotein aggregation
000004685 65320 $$2Author$$adomain interaction
000004685 65320 $$2Author$$aco-translational folding
000004685 65320 $$2Author$$asingle molecule studies
000004685 65320 $$2Author$$afluorescence correlation spectroscopy
000004685 773__ $$0PERI:(DE-600)1458497-9$$a10.1007/s00018-009-8771-9$$gVol. 66, p. 1672 - 1681$$p1672 - 1681$$q66<1672 - 1681$$tCellular and molecular life sciences$$v66$$x1420-682X$$y2009
000004685 8567_ $$uhttp://dx.doi.org/10.1007/s00018-009-8771-9
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000004685 9141_ $$aNO 3 ist übergangsweise die Bezeichnung des FE-Vorhabens für das ISB-2$$y2009
000004685 915__ $$0StatID:(DE-HGF)0010$$aJCR/ISI refereed
000004685 9201_ $$0I:(DE-Juel1)ISB-2-20090406$$d31.12.2010$$gISB$$kISB-2$$lMolekulare Biophysik$$x0
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