ArticlePloS one2013
Hydrogen bond strengths in phosphorylated and sulfated amino acid residues.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers, 1 of them a synthesis that pooled it.
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Who cites it
12 citing papers in PubMed, 1 synthesis or guideline pooled it, 26 citations in OpenAlex.
- A potential antibody repertoire diversification mechanism through tyrosine sulfation for biotherapeutics engineering and production.Frontiers in immunology · 2022Pooled it
- Custom Workflow for the Confident Identification of Sulfotyrosine-Containing Peptides and Their Discrimination from Phosphopeptides.Journal of proteome research · 2023Article
- Cysteine Oxidation in Proteins: Structure, Biophysics, and Simulation.Biochemistry · 2022Review
- Engineering of a Small Protein Scaffold To Recognize Sulfotyrosine with High Specificity.ACS chemical biology · 2021Article
- Emerging patterns of tyrosine sulfation and O-glycosylation cross-talk and co-localization.Current opinion in structural biology · 2020Review
- Protein Interaction with Charged Macromolecules: From Model Polymers to Unfolded Proteins and Post-Translational Modifications.International journal of molecular sciences · 2019Review
- Characterization of the APLF FHA-XRCC1 phosphopeptide interaction and its structural and functional implications.Nucleic acids research · 2017Article
- CCR7 Sulfotyrosine Enhances CCL21 Binding.International journal of molecular sciences · 2017Article
- Effects of pseudophosphorylation mutants on the structural dynamics of smooth muscle myosin regulatory light chain.Molecular bioSystems · 2014Article
- Gas-phase intermolecular phosphate transfer within a phosphohistidine phosphopeptide dimer.International journal of mass spectrometry · 2014Article
- Active site conformational dynamics are coupled to catalysis in the mRNA decapping enzyme Dcp2.Structure (London, England : 1993) · 2013Article
- The role of tyrosine sulfation in the dimerization of the CXCR4:SDF-1 complex.Protein science : a publication of the Protein Society · 2013Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Post-translational modification by the addition of an oxoanion functional group, usually a phosphate group and less commonly a sulfate group, leads to diverse structural and functional consequences in protein systems. Building upon previous studies of the phosphoserine residue (pSer), we address the distinct nature of hydrogen bonding interactions in phosphotyrosine (pTyr) and sulfotyrosine (sTyr) residues. We derive partial charges for these modified residues and then study them in the context of molecular dynamics simulation of model tripeptides and sulfated protein complexes, potentials of mean force for interacting residue pairs, and a survey of the interactions of modified residues among experimental protein structures. Overall, our findings show that for pTyr, bidentate interactions with Arg are particularly dominant, as has been previously demonstrated for pSer. sTyr interactions with Arg are significantly weaker, even as compared to the same interactions made by the Glu residue. Our work sheds light on the distinct nature of these modified tyrosine residues, and provides a physical-chemical foundation for future studies with the goal of understanding their roles in systems of biological interest.
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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.