{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["120(8)"],"submitter":["Aplin CP"],"funding":["Dutch Research Council (NWO)"],"pubmed_abstract":["Eukaryotic cells exploit dynamic and compartmentalized ionic strength to impact a myriad of biological functions such as enzyme activities, protein-protein interactions, and catalytic functions. Herein, we investigated the fluorescence depolarization dynamics of recently developed ionic strength biosensors (mCerulean3-linker-mCitrine) in Hofmeister salt (KCl, NaCl, NaI, and Na<sub>2</sub>SO<sub>4</sub>) solutions. The mCerulean3-mCitrine acts as a Förster resonance energy transfer (FRET) pair, tethered together by two oppositely charged α-helices in the linker region. We developed a time-resolved fluorescence depolarization anisotropy approach for FRET analyses, in which the donor (mCerulean3) is excited by 425-nm laser pulses, followed by fluorescence depolarization analysis of the accept"],"journal":["Biophysical journal"],"pagination":["1417-1430"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8105717"],"repository":["biostudies-literature"],"pubmed_title":["Fluorescence depolarization dynamics of ionic strength sensors using time-resolved anisotropy."],"pmcid":["PMC8105717"],"pubmed_authors":["Aplin CP","Heikal AA","Miller RC","Sheets ED","Boersma AJ","Kay TM"],"additional_accession":[]},"is_claimable":false,"name":"Fluorescence depolarization dynamics of ionic strength sensors using time-resolved anisotropy.","description":"Eukaryotic cells exploit dynamic and compartmentalized ionic strength to impact a myriad of biological functions such as enzyme activities, protein-protein interactions, and catalytic functions. Herein, we investigated the fluorescence depolarization dynamics of recently developed ionic strength biosensors (mCerulean3-linker-mCitrine) in Hofmeister salt (KCl, NaCl, NaI, and Na<sub>2</sub>SO<sub>4</sub>) solutions. The mCerulean3-mCitrine acts as a Förster resonance energy transfer (FRET) pair, tethered together by two oppositely charged α-helices in the linker region. We developed a time-resolved fluorescence depolarization anisotropy approach for FRET analyses, in which the donor (mCerulean3) is excited by 425-nm laser pulses, followed by fluorescence depolarization analysis of the accept","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Apr","modification":"2025-04-04T19:41:34.504Z","creation":"2025-04-04T19:41:34.504Z"},"accession":"S-EPMC8105717","cross_references":{"pubmed":["33582140"],"doi":["10.1016/j.bpj.2021.01.035"]}}