ArticleBiophysical journal2021
Quantifying charge state heterogeneity for proteins with multiple ionizable residues.
Article in Biophysical journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 42 citations in OpenAlex.
- Mapping Charge Interactions in Intrinsically Disordered Proteins.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Statistical Physics-Based Approaches to Model the Function and Complexation of Disordered Proteins.The journal of physical chemistry. B · 2025Article
- A pH-Centric Model of Nucleolar Activity and Regulation.Journal of molecular biology · 2025Review
- FINCHES: A Computational Framework for Predicting Intermolecular Interactions in Intrinsically Disordered Proteins.International journal of molecular sciences · 2025Review
- MEDOC: A Fast, Scalable, and Mathematically Exact Algorithm for the Site-Specific Prediction of the Protonation Degree in Large Disordered Proteins.Journal of chemical information and modeling · 2025Article
- Phosphorylation of disordered proteins tunes local and global intramolecular interactions.Biophysical journal · 2024Article
- Emergent microenvironments of nucleoli.Nucleus (Austin, Tex.) · 2024Review
- A Few Charged Residues in Galectin-3's Folded and Disordered Regions Regulate Phase Separation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Biomolecular Condensates are Characterized by Interphase Electric Potentials.Journal of the American Chemical Society · 2024Article
- Beyond monopole electrostatics in regulating conformations of intrinsically disordered proteins.PNAS nexus · 2024Article
- Phosphorylation of disordered proteins tunes local and global intramolecular interactions.bioRxiv : the preprint server for biology · 2024Article
- Direct prediction of intermolecular interactions driven by disordered regions.bioRxiv : the preprint server for biology · 2024Article
- Article
- Liquid-liquid phase separation driven by charge heterogeneity.Communications physics · 2024Article
- Electric Potential at the Interface of Membraneless Organelles Gauged by Graphene.Nano letters · 2023Article
- Intrinsically disordered regions are poised to act as sensors of cellular chemistry.Trends in biochemical sciences · 2023Review
- Driving forces of the complex formation between highly charged disordered proteins.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Pervasive, conserved secondary structure in highly charged protein regions.PLoS computational biology · 2023Article
- Dissecting the phase separation and oligomerization activities of the carboxysome positioning protein McdB.eLife · 2023Article
- Phase Transitions of Associative Biomacromolecules.Chemical reviews · 2023Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Ionizable residues can release and take up protons and this has an influence on protein structure and function. The extent of protonation is linked to the overall pH of the solution and the local environments of ionizable residues. Binding or unbinding of a single proton generates a distinct charge microstate defined by a specific pattern of charges. Accordingly, the overall partition function is a sum over all charge microstates and Boltzmann weights of all conformations associated with each of the charge microstates. This ensemble-of-ensembles description recast as a q-canonical ensemble allows us to analyze and interpret potentiometric titrations that provide information regarding net charge as a function of pH. In the q-canonical ensemble, charge microstates are grouped into mesostates where each mesostate is a collection of microstates of the same net charge. Here, we show that leveraging the structure of the q-canonical ensemble allows us to decouple contributions of net proton binding and release from proton arrangement and conformational considerations. Through application of the q-canonical formalism to analyze potentiometric measurements of net charge in proteins with repetitive patterns of Lys and Glu residues, we determine the underlying mesostate pK
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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.