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  SNARE assembly and disassembly exhibit a pronounced hysteresis

Fasshauer, D., Antonin, W., Subramaniam, V., & Jahn, R. (2002). SNARE assembly and disassembly exhibit a pronounced hysteresis. Nature Structural Biology, 9(2), 144-151. Retrieved from http://www.nature.com/nsmb/journal/v9/n2/pdf/nsb750.pdf.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-F454-A Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-8F9B-B
Genre: Journal Article

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599701.pdf (Publisher version), 921KB
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 Creators:
Fasshauer, D.1, Author              
Antonin, W.2, Author              
Subramaniam, V.3, Author              
Jahn, R.2, Author              
Affiliations:
1Research Group of Structural Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578596              
2Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society, ou_578595              
3Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society, ou_578628              

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 Abstract: SNARE proteins are essential for intracellular membrane fusion of eukaryotes. Their assembly into stable four-helix bundles bridges membranes and may provide the energy for initiating membrane fusion. In vitro, assembly of soluble SNARE fragments is accompanied by major structural rearrangements that can be described as a folding reaction. The pathways and the thermodynamics of SNARE protein interactions, however, are not known. Here we report that assembly and dissociation of two distantly related SNARE complexes exhibit a marked hysteresis. The assembled and disassembled native states are separated by a kinetic barrier and cannot equilibrate on biologically relevant timescales. We suggest that the hysteresis is a hallmark of all SNARE complexes and that complex assembly and disassembly follow different pathways that may be independently controlled.

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Language(s): eng - English
 Dates: 2002-02
 Publication Status: Published in print
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 Rev. Method: Peer
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Title: Nature Structural Biology
Source Genre: Journal
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Pages: - Volume / Issue: 9 (2) Sequence Number: - Start / End Page: 144 - 151 Identifier: -