ArticleNature methods2022
Monitoring protein conformational changes using fluorescent nanoantennas.
Article in Nature methods, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Effects of Arginine on Hierarchical Protein Aggregation.The protein journal · 2026Article
- Single molecule spectrum dynamics imaging with 3D target-locking tracking.Nature communications · 2025Article
- Critical assessment of selenourea as an efficient small molecule fluorescence quenching probe to monitor protein dynamics.Chemical science · 2023Article
- Kinetic data for modeling the dynamics of the enzymes involved in animal fatty acid synthesis.Bioscience reports · 2023Review
- Applications of fluorescence spectroscopy in protein conformational changes and intermolecular contacts.BBA advances · 2023Article
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Understanding the relationship between protein structural dynamics and function is crucial for both basic research and biotechnology. However, methods for studying the fast dynamics of structural changes are limited. Here, we introduce fluorescent nanoantennas as a spectroscopic technique to sense and report protein conformational changes through noncovalent dye-protein interactions. Using experiments and molecular simulations, we detect and characterize five distinct conformational states of intestinal alkaline phosphatase, including the transient enzyme-substrate complex. We also explored the universality of the nanoantenna strategy with another model protein, Protein G and its interaction with antibodies, and demonstrated a rapid screening strategy to identify efficient nanoantennas. These versatile nanoantennas can be used with diverse dyes to monitor small and large conformational changes, suggesting that they could be used to characterize diverse protein movements or in high-throughput screening applications.
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Registered trials
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