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J Am Chem Soc. 2013 Jul 17;135(28):10254-7. doi: 10.1021/ja404276g. Epub 2013 Jul 9.

Real-time observation of multiple-protein complex formation with single-molecule FRET.

Author information

1
National Creative Research Initiative Center for Single-Molecule Systems Biology and Department of Physics, KAIST, Daejeon 305-701, South Korea.

Erratum in

  • J Am Chem Soc. 2013 Oct 30;135(43):16242. Bae, Woori [corrected to Bae, Wooli].

Abstract

Current single-molecule techniques do not permit the real-time observation of multiple proteins interacting closely with each other. We here report an approach enabling us to determine the single-molecule fluorescence resonance energy transfer (FRET) kinetics of multiple protein-protein interactions occurring far below the diffraction limit. We observe a strongly cooperative formation of multimeric soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complexes, which suggests that formation of the first SNARE complex triggers a cascade of SNARE complex formation.

PMID:
23808880
PMCID:
PMC3773174
DOI:
10.1021/ja404276g
[Indexed for MEDLINE]
Free PMC Article

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