ArticleProtein science : a publication of the Protein Society2020
Discriminating changes in protein structure using tyrosine conjugation.
Article in Protein science : a publication of the Protein Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 30 citations in OpenAlex.
- Recent Advances in Bioconjugation of Aromatic Amino Acid Residues by a Reactivity-Guided Approach.Chemical record (New York, N.Y.) · 2026Review
- Bovine Serum Albumin-Trypsin Sponges for Enhanced Enzymatic Stability and Protein Digestion Efficiency.ACS applied bio materials · 2025Article
- Advancing Covalent Ligand and Drug Discovery beyond Cysteine.Chemical reviews · 2025Review
- Purification of Low-Complexity Domain Proteins FUS, EWSR1, and Their Fusions.Current protocols · 2025Article
- The potential of the South African plant Tulbaghia Violacea Harv for the treatment of triple negative breast cancer.Scientific reports · 2025Article
- Mechanical Properties of Protein-Based Hydrogels Derived from Binary Protein Mixtures-A Feasibility Study.Polymers · 2023Article
- Triazolinedione protein modification: from an overlooked off-target effect to a tryptophan-based bioconjugation strategy.Chemical science · 2022Article
- Changing mechanical properties of photopolymerized, dityrosine-crosslinked protein-based hydrogels.Frontiers in bioengineering and biotechnology · 2022Article
- Injectable niclosamide nanohybrid as an anti-SARS-CoV-2 strategy.Colloids and surfaces. B, Biointerfaces · 2021Article
- Luminol anchors improve the electrochemical-tyrosine-click labelling of proteins.Chemical science · 2021Article
- Evaluation of the potency of FDA-approved drugs on wild type and mutant SARS-CoV-2 helicase (Nsp13).International journal of biological macromolecules · 2020Article
- Discriminating changes in protein structure using tyrosine conjugation.Protein science : a publication of the Protein Society · 2020Article
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Authors and funding
6 authors at 1 institution in 1 country.
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Abstract
Chemical modification of proteins has been crucial in engineering protein-based therapies, targeted biopharmaceutics, molecular probes, and biomaterials. Here, we explore the use of a conjugation-based approach to sense alternative conformational states in proteins. Tyrosine has both hydrophobic and hydrophilic qualities, thus allowing it to be positioned at protein surfaces, or binding interfaces, or to be buried within a protein. Tyrosine can be conjugated with 4-phenyl-3H-1,2,4-triazole-3,5(4H)-dione (PTAD). We hypothesized that individual protein conformations could be distinguished by labeling tyrosine residues in the protein with PTAD. We conjugated tyrosine residues in a well-folded protein, bovine serum albumin (BSA), and quantified labeled tyrosine with liquid chromatography with tandem mass spectrometry. We applied this approach to alternative conformations of BSA produced in the presence of urea. The amount of PTAD labeling was found to relate to the depth of each tyrosine relative to the protein surface. This study demonstrates a new use of tyrosine conjugation using PTAD as an analytic tool able to distinguish the conformational states of a protein.
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