ArticleChembiochem : a European journal of chemical biology2016
Dual Unnatural Amino Acid Incorporation and Click-Chemistry Labeling to Enable Single-Molecule FRET Studies of p97 Folding.
Article in Chembiochem : a European journal of chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 29 citations in OpenAlex.
- Dynamic positioning of Rpc34 winged helix in RNA polymerase III elongation complex for its stability with implications for reinitiation.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Development and Optimization of an Aminooxy Coupling Reaction to Prepare Multivalent Bioconjugates with a Single Noncanonical Amino Acid.Bioconjugate chemistry · 2026Article
- Labelizer: systematic selection of protein residues for covalent fluorophore labeling.Nature communications · 2025Article
- Surface Functionalization of Elastomers with Biopolymers.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Growth hormone receptor agonists and antagonists: From protein expression and purification to long-acting formulations.Protein science : a publication of the Protein Society · 2023Review
- Site-specific incorporation of biophysical probes into NF-ĸB with non-canonical amino acids.Methods (San Diego, Calif.) · 2023Article
- Cross-validation of distance measurements in proteins by PELDOR/DEER and single-molecule FRET.Nature communications · 2022Article
- Structural Dynamics of Glutamate Signaling Systems by smFRET.Biophysical journal · 2020Review
- Ratiometric Single-Molecule FRET Measurements to Probe Conformational Subpopulations of Intrinsically Disordered Proteins.Current protocols in chemical biology · 2020Article
- Single-molecule fluorescence studies of intrinsically disordered proteins and liquid phase separation.Biochimica et biophysica acta. Proteins and proteomics · 2019Review
- Coming Together: RNAs and Proteins Assemble under the Single-Molecule Fluorescence Microscope.Cold Spring Harbor perspectives in biology · 2019Review
- Polymer conjugation of proteins as a synthetic post-translational modification to impact their stability and activity.Polymer chemistry · 2019Article
- Construction of an immunotoxin via site-specific conjugation of anti-Her2 IgG and engineeredJournal of biological engineering · 2019Article
- Expansion of the genetic code via expansion of the genetic alphabet.Current opinion in chemical biology · 2018Review
- "Expand and Click": A New Method for Labeling HIV-1 Envelope Glycoproteins.Cell chemical biology · 2017Article
- Conformational transition of FGFR kinase activation revealed by site-specific unnatural amino acid reporter and single molecule FRET.Scientific reports · 2017Article
- Utilizing functional cell-free extracts to dissect ribonucleoprotein complex biology at single-molecule resolution.Wiley interdisciplinary reviews. RNAReview
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Many cellular functions are critically dependent on the folding of complex multimeric proteins, such as p97, a hexameric multidomain AAA+ chaperone. Given the complex architecture of p97, single-molecule (sm) FRET would be a powerful tool for studying folding while avoiding ensemble averaging. However, dual site-specific labeling of such a large protein for smFRET is a significant challenge. Here, we address this issue by using bioorthogonal azide-alkyne chemistry to attach an smFRET dye pair to site-specifically incorporated unnatural amino acids, allowing us to generate p97 variants reporting on inter- or intradomain structural features. An initial proof-of-principle set of smFRET results demonstrated the strengths of this labeling method. Our results highlight this as a powerful tool for structural studies of p97 and other large protein machines.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.