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  1. Article ; Online: Determining the Functional Oligomeric State of Membrane-Associated Protein Oligomers Forming Membrane Pores on Giant Lipid Vesicles.

    Singh, Vandana / Macharová, Sabína / Riegerová, Petra / Steringer, Julia P / Müller, Hans-Michael / Lolicato, Fabio / Nickel, Walter / Hof, Martin / Šachl, Radek

    Analytical chemistry

    2023  Volume 95, Issue 23, Page(s) 8807–8815

    Abstract: Several peripheral membrane proteins are known to form membrane pores through multimerization. In many cases, in biochemical reconstitution experiments, a complex distribution of oligomeric states has been observed that may, in part, be irrelevant to ... ...

    Abstract Several peripheral membrane proteins are known to form membrane pores through multimerization. In many cases, in biochemical reconstitution experiments, a complex distribution of oligomeric states has been observed that may, in part, be irrelevant to their physiological functions. This phenomenon makes it difficult to identify the functional oligomeric states of membrane lipid interacting proteins, for example, during the formation of transient membrane pores. Using fibroblast growth factor 2 (FGF2) as an example, we present a methodology applicable to giant lipid vesicles by which functional oligomers can be distinguished from nonspecifically aggregated proteins without functionality. Two distinct populations of fibroblast growth factor 2 were identified with (i) dimers to hexamers and (ii) a broad population of higher oligomeric states of membrane-associated FGF2 oligomers significantly distorting the original unfiltered histogram of all detectable oligomeric species of FGF2. The presented statistical approach is relevant for various techniques for characterizing membrane-dependent protein oligomerization.
    MeSH term(s) Cell Membrane/metabolism ; Membrane Proteins/metabolism ; Fibroblast Growth Factor 2/metabolism ; Membranes ; Lipids ; Protein Multimerization
    Chemical Substances Membrane Proteins ; Fibroblast Growth Factor 2 (103107-01-3) ; Lipids
    Language English
    Publishing date 2023-05-06
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1508-8
    ISSN 1520-6882 ; 0003-2700
    ISSN (online) 1520-6882
    ISSN 0003-2700
    DOI 10.1021/acs.analchem.2c05692
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Determining the Functional Oligomeric State of Membrane-Associated Protein Oligomers Forming Membrane Pores on Giant Lipid Vesicles

    Singh, Vandana / Macharová, Sabína / Riegerová, Petra / Steringer, Julia P. / Müller, Hans-Michael / Lolicato, Fabio / Nickel, Walter / Hof, M. / Šachl, Radek

    Analytical Chemistry. 2023 May 06, v. 95, no. 23 p.8807-8815

    2023  

    Abstract: Several peripheral membrane proteins are known to form membrane pores through multimerization. In many cases, in biochemical reconstitution experiments, a complex distribution of oligomeric states has been observed that may, in part, be irrelevant to ... ...

    Abstract Several peripheral membrane proteins are known to form membrane pores through multimerization. In many cases, in biochemical reconstitution experiments, a complex distribution of oligomeric states has been observed that may, in part, be irrelevant to their physiological functions. This phenomenon makes it difficult to identify the functional oligomeric states of membrane lipid interacting proteins, for example, during the formation of transient membrane pores. Using fibroblast growth factor 2 (FGF2) as an example, we present a methodology applicable to giant lipid vesicles by which functional oligomers can be distinguished from nonspecifically aggregated proteins without functionality. Two distinct populations of fibroblast growth factor 2 were identified with (i) dimers to hexamers and (ii) a broad population of higher oligomeric states of membrane-associated FGF2 oligomers significantly distorting the original unfiltered histogram of all detectable oligomeric species of FGF2. The presented statistical approach is relevant for various techniques for characterizing membrane-dependent protein oligomerization.
    Keywords analytical chemistry ; fibroblast growth factor 2 ; lipids ; membrane proteins ; oligomerization ; protein subunits ; statistical analysis
    Language English
    Dates of publication 2023-0506
    Size p. 8807-8815.
    Publishing place American Chemical Society
    Document type Article ; Online
    ZDB-ID 1508-8
    ISSN 1520-6882 ; 0003-2700
    ISSN (online) 1520-6882
    ISSN 0003-2700
    DOI 10.1021/acs.analchem.2c05692
    Database NAL-Catalogue (AGRICOLA)

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