{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Deedwania A"],"funding":["Medical Research Council","Royal Society","Engineering and Physical Sciences Research Council"],"pagination":["120-128"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12560048"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["7(1)"],"pubmed_abstract":["Membrane proteins and lipids are essential for a wide range of cellular processes, making their structural characterisation essential for understanding biological function. However, the amphipathic nature of membrane proteins poses a significant challenge for traditional structural biology techniques. Membrane mimetics offer an alternative approach to studying membrane proteins in more native-like environments. Among them, peptidiscs have emerged as a promising tool for stabilising membrane proteins, allowing reconstitution from detergent micelles into a detergent-free, native-like environment that preserves structural integrity. While peptidiscs have shown utility in techniques such as mass photometry and cryo-EM, their compatibility with native mass spectrometry (MS) remains largely unex"],"journal":["RSC chemical biology"],"pubmed_title":["Native mass spectrometry of membrane proteins reconstituted in peptidiscs."],"pmcid":["PMC12560048"],"funding_grant_id":["MR/V028839/1","URF\\R1\\211567","EP/Y036158/1"],"pubmed_authors":["Deedwania A","Robinson CV","Wang Y","Bolla JR"],"additional_accession":[]},"is_claimable":false,"name":"Native mass spectrometry of membrane proteins reconstituted in peptidiscs.","description":"Membrane proteins and lipids are essential for a wide range of cellular processes, making their structural characterisation essential for understanding biological function. However, the amphipathic nature of membrane proteins poses a significant challenge for traditional structural biology techniques. Membrane mimetics offer an alternative approach to studying membrane proteins in more native-like environments. Among them, peptidiscs have emerged as a promising tool for stabilising membrane proteins, allowing reconstitution from detergent micelles into a detergent-free, native-like environment that preserves structural integrity. While peptidiscs have shown utility in techniques such as mass photometry and cryo-EM, their compatibility with native mass spectrometry (MS) remains largely unex","dates":{"release":"2026-01-01T00:00:00Z","publication":"2026 Jan","modification":"2026-06-13T04:55:31.748Z","creation":"2026-06-13T03:08:59.731Z"},"accession":"S-EPMC12560048","cross_references":{"pubmed":["41164344"],"doi":["10.1039/d5cb00236b"]}}