@inbook{f07750f0c5c74ea7beac61689ed469dc,
title = "Structural Dynamics of SNARE Complex Assembly in the Ribbon Synapses Observed by smFRET",
abstract = "Single-molecule fluorescence resonance energy transfer (smFRET) is a powerful technique for studying the structural dynamics of protein molecules or detecting interactions between protein molecules in real time. Due to the high sensitivity in spatial and temporal resolution, smFRET can decipher sub-populations within heterogeneous native state conformations, which are generally lost in traditional measurements due to ensemble averaging. In addition, the single-molecule reconstitution allows protein molecules to be observed for an extensive period of time and can recapitulate the geometry of the cellular environment to retain biological function. Here we provide a detailed method of using smFRET to monitor the conformational dynamics of syntaxin-3b from the ribbon synapses during assembly of the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex.",
keywords = "Munc18, Phosphorylation, SNARE proteins, Single-molecule FRET, Syntaxin-3b",
author = "Andrzejewski, \{Alexa L.\} and Joshua Ferrar and Marla Kratzer-Charron and Bowen, \{Mark E.\} and Choi, \{Ucheor B.\}",
note = "Publisher Copyright: {\textcopyright} The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature 2025.",
year = "2025",
doi = "10.1007/978-1-0716-4314-3\_13",
language = "English",
series = "Methods in Molecular Biology",
publisher = "Humana Press Inc.",
pages = "185--196",
booktitle = "Methods in Molecular Biology",
}