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Biochemistry

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JoVE Journal Biochemistry
Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One α-Synuclein Monomer at a Time
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Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One α-Synuclein Monomer at a Time

Article DOI: 10.3791/62655-v • 07:56 min • May 30th, 2021
May 30th, 2021 •
1, 1,2
1Department of Biological Chemistry, The Alexander Silberman Institute of Life Sciences, Faculty of Mathematics & Science, The Edmond J. Safra Campus, The Hebrew University of Jerusalem, 2The Center for Nanoscience and Nanotechnology, The Hebrew University of Jerusalem

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Time-resolved single-molecule protein-induced fluorescence enhancement is a useful fluorescence spectroscopic proximity sensor sensitive to local structural changes in proteins. Here we show it can be used to uncover stable local conformations in α-Synuclein, which is otherwise known as globularly unstructured and unstable when measured using the longer range FRET ruler.

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Time-resolved Protein-induced Fluorescence Enhancement Stable Local Conformations α-Synuclein Monomer Single-molecule FRET Measurements Protein Structural Subpopulations Distinct Site-specific Structural Subpopulations Biomolecular System Sulfo-Cy3-labeled α-synuclein Measurement Buffer Low-protein Binding Tube BSA 18-chamber Microscopy Cover Slide Data Acquisition High-numerical-aperture Water Immersion Objective Lens Microscope Stage
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