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The Analysis of In-Membrane Nanoscopic Aggregation of Lipids and Proteins by MC-FRET

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388955%3A_____%2F23%3A00571347" target="_blank" >RIV/61388955:_____/23:00571347 - isvavai.cz</a>

  • Alternative codes found

    RIV/61388963:_____/23:00571347 RIV/00216208:11320/22:10447432

  • Result on the web

    <a href="http://dx.doi.org/10.1007/4243_2022_29" target="_blank" >http://dx.doi.org/10.1007/4243_2022_29</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1007/4243_2022_29" target="_blank" >10.1007/4243_2022_29</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    The Analysis of In-Membrane Nanoscopic Aggregation of Lipids and Proteins by MC-FRET

  • Original language description

    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.

  • Czech name

  • Czech description

Classification

  • Type

    C - Chapter in a specialist book

  • CEP classification

  • OECD FORD branch

    10403 - Physical chemistry

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2023

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Book/collection name

    Fluorescence spectroscopy and microscopy in biology

  • ISBN

    978-3-031-30361-6

  • Number of pages of the result

    26

  • Pages from-to

    375-400

  • Number of pages of the book

    532

  • Publisher name

    Springer Nature

  • Place of publication

    Chum

  • UT code for WoS chapter