Interplay between conformational dynamics and substrate binding regulates enzymatic activity: a single-molecule FRET study Article Swipe

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David Scheerer , Dorit Levy , Remi Casier , Inbal Riven , Hisham Mazal , Gilad Haran ·

YOU? · · 2025 · Open Access · · DOI: https://doi.org/10.1039/d4sc06819j

Single-molecule FRET reveals urea-induced conformational shifts in adenylate kinase, enhancing activity through promoting the open conformation and efficient substrate positioning.

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Förster resonance energy transfer Single-molecule FRET Substrate (aquarium) Chemistry Biophysics Enzyme Dynamics (music) Molecule Conformational change Molecular dynamics Stereochemistry Computational chemistry Biochemistry Biology Fluorescence Physics Acoustics Ecology Organic chemistry Quantum mechanics

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Type: article
Language: en
Landing Page: https://doi.org/10.1039/d4sc06819j
OA Status: diamond
Cited By: 8
References: 65
Related Works: 10
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DOI: https://doi.org/10.1039/d4sc06819j

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Title: Interplay between conformational dynamics and substrate binding regulates enzymatic activity: a single-molecule FRET study

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Language: en

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Publication year: 2025

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Publication date: 2025-01-01

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Authors: David Scheerer, Dorit Levy, Remi Casier, Inbal Riven, Hisham Mazal, Gilad Haran

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Landing page: https://doi.org/10.1039/d4sc06819j

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Concepts: Förster resonance energy transfer, Single-molecule FRET, Substrate (aquarium), Chemistry, Biophysics, Enzyme, Dynamics (music), Molecule, Conformational change, Molecular dynamics, Stereochemistry, Computational chemistry, Biochemistry, Biology, Fluorescence, Physics, Acoustics, Ecology, Organic chemistry, Quantum mechanics

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Cited by: 8

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