<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Toyama Y</submitter><funding>CIHR</funding><pagination>e2210492119</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9457416</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>119(36)</volume><pubmed_abstract>Electrostatic interactions and charge balance are important for the formation of biomolecular condensates involving proteins and nucleic acids. However, a detailed, atomistic picture of the charge distribution around proteins during the phase-separation process is lacking. Here, we use solution NMR spectroscopy to measure residue-specific near-surface electrostatic potentials (&lt;i>ϕ&lt;/i>&lt;sub>ENS&lt;/sub>) of the positively charged carboxyl-terminal intrinsically disordered 103 residues of CAPRIN1, an RNA-binding protein localized to membraneless organelles playing an important role in messenger RNA (mRNA) storage and translation. Measured &lt;i>ϕ&lt;/i>&lt;sub>ENS&lt;/sub> values have been mapped along the adenosine triphosphate (ATP)-induced phase-separation trajectory. In the absence of ATP, &lt;i>ϕ&lt;/i>&lt;sub</pubmed_abstract><journal>Proceedings of the National Academy of Sciences of the United States of America</journal><pubmed_title>Mapping the per-residue surface electrostatic potential of CAPRIN1 along its phase-separation trajectory.</pubmed_title><pmcid>PMC9457416</pmcid><funding_grant_id>FND-148375</funding_grant_id><funding_grant_id>FND-503573</funding_grant_id><pubmed_authors>Toyama Y</pubmed_authors><pubmed_authors>Forman-Kay JD</pubmed_authors><pubmed_authors>Rangadurai AK</pubmed_authors><pubmed_authors>Kay LE</pubmed_authors></additional><is_claimable>false</is_claimable><name>Mapping the per-residue surface electrostatic potential of CAPRIN1 along its phase-separation trajectory.</name><description>Electrostatic interactions and charge balance are important for the formation of biomolecular condensates involving proteins and nucleic acids. However, a detailed, atomistic picture of the charge distribution around proteins during the phase-separation process is lacking. Here, we use solution NMR spectroscopy to measure residue-specific near-surface electrostatic potentials (&lt;i>ϕ&lt;/i>&lt;sub>ENS&lt;/sub>) of the positively charged carboxyl-terminal intrinsically disordered 103 residues of CAPRIN1, an RNA-binding protein localized to membraneless organelles playing an important role in messenger RNA (mRNA) storage and translation. Measured &lt;i>ϕ&lt;/i>&lt;sub>ENS&lt;/sub> values have been mapped along the adenosine triphosphate (ATP)-induced phase-separation trajectory. In the absence of ATP, &lt;i>ϕ&lt;/i>&lt;sub</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022 Sep</publication><modification>2026-05-27T21:06:27.035Z</modification><creation>2025-04-25T16:55:51.218Z</creation></dates><accession>S-EPMC9457416</accession><cross_references><pubmed>36040869</pubmed><doi>10.1073/pnas.2210492119</doi></cross_references></HashMap>