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KERA: analysis tool for multi-process, multi-state single-molecule data
Journal article   Open access   Peer reviewed

KERA: analysis tool for multi-process, multi-state single-molecule data

Joseph Tibbs, Mohamed Ghoneim, Colleen C. Caldwell, Troy Buzynski, Wayne Bowie, Elizabeth M. Boehm, M. Todd Washington, S. M. Ali Tabei and Maria Spies
Nucleic acids research, Vol.49(9), pp.e53-e53
05/21/2021
DOI: 10.1093/nar/gkab087
PMCID: PMC8136784
PMID: 33660771
url
https://doi.org/10.1093/nar/gkab087View
Published (Version of record) Open Access

Abstract

Molecular machines within cells dynamically assemble, disassemble and reorganize. Molecular interactions between their components can be observed at the single-molecule level and quantified using colocalization single-molecule spectroscopy, in which individual labeled molecules are seen transiently associating with a surface-tethered partner, or other total internal reflection fluorescence microscopy approaches in which the interactions elicit changes in fluorescence in the labeled surface-tethered partner. When multiple interacting partners can form ternary, quaternary and higher order complexes, the types of spatial and temporal organization of these complexes can be deduced from the order of appearance and reorganization of the components. Time evolution of complex architectures can be followed by changes in the fluorescence behavior in multiple channels. Here, we describe the kinetic event resolving algorithm (KERA), a software tool for organizing and sorting the discretized fluorescent trajectories from a range of single-molecule experiments. KERA organizes the data in groups by transition patterns, and displays exhaustive dwell time data for each interaction sequence. Enumerating and quantifying sequences of molecular interactions provides important information regarding the underlying mechanism of the assembly, dynamics and architecture of the macromolecular complexes. We demonstrate KERA's utility by analyzing conformational dynamics of two DNA binding proteins: replication protein A and xeroderma pigmentosum complementation group D helicase.
Biochemistry & Molecular Biology Life Sciences & Biomedicine Science & Technology

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