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- W2115690303 abstract "Abstract Here we study the intact stoichiometry and top‐down fragmentation behavior of three integral membrane proteins which were natively reconstituted into detergent micelles: the mechano‐sensitive ion channel of large conductance (MscL), the Kirbac potassium channel and the p7 viroporin from the hepatitis C virus. By releasing the proteins under nondenaturing conditions inside the mass spectrometer, we obtained their oligomeric sizes. Increasing the ion activation (collision energy) causes unfolding and subsequent ejection of a highly charged monomer from the membrane protein complexes. Further increase of the ion activation then causes collision‐induced dissociation (CID) of the ejected monomers, with fragments observed which were predominantly found to stem from membrane‐embedded regions. These experiments show how in a single experiment, we can probe the relation between higher‐order structure and protein sequence, by combining the native MS data with fragmentation obtained from top‐down MS." @default.
- W2115690303 created "2016-06-24" @default.
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- W2115690303 date "2015-05-29" @default.
- W2115690303 modified "2023-10-14" @default.
- W2115690303 title "Top-down mass spectrometry of intact membrane protein complexes reveals oligomeric state and sequence information in a single experiment" @default.
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- W2115690303 doi "https://doi.org/10.1002/pro.2703" @default.
- W2115690303 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4534180" @default.
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- W2115690303 hasPublicationYear "2015" @default.
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