Number of the records: 1  

Fluorescence spectroscopy and microscopy in biology

  1. 1.
    0571347 - ÚFCH JH 2024 RIV CH eng M - Monography Chapter
    Chmelová, Barbora - Humpolíčková, Jana - Stříšovský, Kvido - Šachl, Radek
    The Analysis of In-Membrane Nanoscopic Aggregation of Lipids and Proteins by MC-FRET.
    Fluorescence spectroscopy and microscopy in biology. Chum: Springer Nature, 2023 - (Šachl, R.; Amaro, M.), s. 375-400. Springer Series on Fluorescence, 20. ISBN 978-3-031-30361-6
    R&D Projects: GA ČR(CZ) GC20-01401J; GA ČR(CZ) GA19-18917S; GA ČR(CZ) GA18-09556S; GA MŠMT(CZ) EF16_019/0000729
    Institutional support: RVO:61388955 ; RVO:61388963
    Keywords : dimers * MC-FRET * gangliosides
    OECD category: Physical chemistry; Biochemistry and molecular biology (UOCHB-X)

    Many lipids and membrane proteins spontaneously co-cluster and oligomerize in cellular plasma membranes into larger (functional) units, whose detailed characterization requires high spatial resolution. In this contribution, we introduce a powerful spectroscopy/microscopy approach called MC-FRET developed for the analysis of in-membrane nanoscopic aggregation of lipids and proteins in biological membranes. The approach is based on Förster resonance energy transfer (FRET) occurring in membranes between fluorescently labelled lipids/proteins and subsequent analysis of data by Monte-Carlo simulations. The following applications of MC-FRET are presented here: (1) determination of lipid nanodomain sizes and their surface density, (2) characterization of inter-leaflet organization of lipid nanodomains and (3) the analysis of dimerization of in-membrane proteins.
    Permanent Link: https://hdl.handle.net/11104/0342587

     
    FileDownloadSizeCommentaryVersionAccess
    0571347.pdf11.3 MBPublisher’s postprintrequire
     
Number of the records: 1  

  This site uses cookies to make them easier to browse. Learn more about how we use cookies.