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

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.

SUBMITTER: Bae W

PROVIDER: S-EPMC3773174 | biostudies-literature | 2013 Jul

REPOSITORIES: biostudies-literature

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

Bae Wooli W Bae Woori W Choi Mal-Gi MG Hyeon Changbong C Shin Yeon-Kyun YK Yoon Tae-Young TY

Journal of the American Chemical Society 20130709 28

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 sug ...[more]

PMID: 23808880

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