{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Toyama Y"],"funding":["CIHR"],"pagination":["e2210492119"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9457416"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["119(36)"],"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 (<i>ϕ</i><sub>ENS</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 <i>ϕ</i><sub>ENS</sub> values have been mapped along the adenosine triphosphate (ATP)-induced phase-separation trajectory. In the absence of ATP, <i>ϕ</i><sub"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["Mapping the per-residue surface electrostatic potential of CAPRIN1 along its phase-separation trajectory."],"pmcid":["PMC9457416"],"funding_grant_id":["FND-148375","FND-503573"],"pubmed_authors":["Toyama Y","Forman-Kay JD","Rangadurai AK","Kay LE"],"additional_accession":[]},"is_claimable":false,"name":"Mapping the per-residue surface electrostatic potential of CAPRIN1 along its phase-separation trajectory.","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 (<i>ϕ</i><sub>ENS</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 <i>ϕ</i><sub>ENS</sub> values have been mapped along the adenosine triphosphate (ATP)-induced phase-separation trajectory. In the absence of ATP, <i>ϕ</i><sub","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Sep","modification":"2026-05-27T21:06:27.035Z","creation":"2025-04-25T16:55:51.218Z"},"accession":"S-EPMC9457416","cross_references":{"pubmed":["36040869"],"doi":["10.1073/pnas.2210492119"]}}