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  Single-molecule fluorescence resonance energy transfer reveals a dynamic equilibrium between closed and open conformations of syntaxin 1

Margittai, M., Widengren, J., Schweinberger, E., Schroeder, G., Felekyan, S., Haustein, E., et al. (2003). Single-molecule fluorescence resonance energy transfer reveals a dynamic equilibrium between closed and open conformations of syntaxin 1. Proceedings of the National Academy of Sciences of the United States of America, 100(26), 15516-15521. Retrieved from http://www.pnas.org/content/100/26/15516.full.pdf+html.

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Margittai, M.1, Author           
Widengren, J.2, Author           
Schweinberger, E.2, Author           
Schroeder, G.3, Author           
Felekyan, S.2, Author           
Haustein, E.4, Author           
Koenig, M.2, Author           
Fasshauer, D.1, Author           
Grubmueller, H.3, Author           
Jahn, R.1, Author           
Seidel, C.2, Author           
Affiliations:
1Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society, ou_578595              
2Department of Spectroscopy and Photochemical Kinetics, MPI for biophysical chemistry, Max Planck Society, ou_578624              
3Research Group of Theoretical Molecular Biophysics, MPI for biophysical chemistry, Max Planck Society, ou_578630              
4Research Group of Experimental Biophysics, MPI for biophysical chemistry, Max Planck Society, ou_578554              

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 Abstract: Protein conformational transitions form the molecular basis of many cellular processes, such as signal transduction and membrane traffic. However, in many cases, little is known about their structural dynamics. Here we have used dynamic single-molecule fluorescence to study at high time resolution, conformational transitions of syntaxin 1, a soluble N-ethylmaleimide-sensitive factor attachment protein receptors protein essential for exocytotic membrane fusion. Sets of syntaxin double mutants were randomly labeled with a mix of donor and acceptor dye and their fluorescence resonance energy transfer was measured. For each set, all fluorescence information was recorded simultaneously with high time resolution, providing detailed information on distances and dynamics that were used to create structural models. We found that free syntaxin switches between an inactive closed and an active open configuration with a relaxation time of 0.8 ms, explaining why regulatory proteins are needed to arrest the protein in one conformational state.

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Language(s): eng - English
 Dates: 2003-12-23
 Publication Status: Published in print
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 Rev. Type: Peer
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Title: Proceedings of the National Academy of Sciences of the United States of America
Source Genre: Journal
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Pages: - Volume / Issue: 100 (26) Sequence Number: - Start / End Page: 15516 - 15521 Identifier: -