ArticleProceedings of the National Academy of Sciences of the United States of America2009
Short-distance probes for protein backbone structure based on energy transfer between bimane and transition metal ions.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed.
- Article
- A PIP2-stabilized syntaxin-1a structure mapped with transition metal ion FRET and unnatural fluorescent amino acids at the plasma membrane.Structure (London, England : 1993) · 2026Article
- Interrogating the structure and function of the human voltage-gated proton channel (hHbioRxiv : the preprint server for biology · 2025Article
- Voltage-clamp fluorometry for advancing mechanistic understanding of ion channel mechanisms with a focus on acid-sensing ion channels.Biochemical Society transactions · 2024Review
- Highly tunable bimane-based fluorescent probes: design, synthesis, and application as a selective amyloid binding dye.Chemical science · 2024Article
- Fluorescent Probes and Quenchers in Studies of Protein Folding and Protein-Lipid Interactions.Chemical record (New York, N.Y.) · 2024Review
- Exploring the KeLife · 2024Article
- Detecting in-solution conformational changes in viral fusogens using tryptophan-induced fluorescence quenching.STAR protocols · 2021Article
- Article
- Article
- Visible-to-NIR-Light Activated Release: From Small Molecules to Nanomaterials.Chemical reviews · 2020Article
- Genetically Encoded Quinone Methides Enabling Rapid, Site-Specific, and Photocontrolled Protein Modification with Amine Reagents.Journal of the American Chemical Society · 2020Article
- Metal Bridge in S4 Segment Supports Helix Transition in Shaker Channel.Biophysical journal · 2020Article
- The contribution of voltage clamp fluorometry to the understanding of channel and transporter mechanisms.The Journal of general physiology · 2019Review
- The HCN channel voltage sensor undergoes a large downward motion during hyperpolarization.Nature structural & molecular biology · 2019Article
- Site-Directed Fluorescence Approaches for Dynamic Structural Biology of Membrane Peptides and Proteins.Frontiers in molecular biosciences · 2019Review
- Article
- Voltage-clamp Fluorometry in Xenopus Oocytes Using Fluorescent Unnatural Amino Acids.Journal of visualized experiments : JoVE · 2017Article
- Article
- Investigating cyclic nucleotide and cyclic dinucleotide binding to HCN channels by surface plasmon resonance.PloS one · 2017Article
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Authors and funding
3 authors.
Funding
Abstract
The structure and dynamics of proteins underlies the workings of virtually every biological process. Existing biophysical methods are inadequate to measure protein structure at atomic resolution, on a rapid time scale, with limited amounts of protein, and in the context of a cell or membrane. FRET can measure distances between two probes, but depends on the orientation of the probes and typically works only over long distances comparable with the size of many proteins. Also, common probes used for FRET can be large and have long, flexible attachment linkers that position dyes far from the protein backbone. Here, we improve and extend a fluorescence method called transition metal ion FRET that uses energy transfer to transition metal ions as a reporter of short-range distances in proteins with little orientation dependence. This method uses a very small cysteine-reactive dye monobromobimane, with virtually no linker, and various transition metal ions bound close to the peptide backbone as the acceptor. We show that, unlike larger fluorophores and longer linkers, this donor-acceptor pair accurately reports short-range distances and changes in backbone distances. We further extend the method by using cysteine-reactive metal chelators, which allow the technique to be used in protein regions of unknown secondary structure or when native metal ion binding sites are present. This improved method overcomes several of the key limitations of classical FRET for intramolecular distance measurements.
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