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Determining the Functional Oligomeric State of Membrane- Associated Protein Oligomers Forming Membrane Pores on Giant Lipid Vesicles

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388955%3A_____%2F23%3A00572771" target="_blank" >RIV/61388955:_____/23:00572771 - isvavai.cz</a>

  • Alternative codes found

    RIV/00216208:11320/23:10464122

  • Result on the web

    <a href="https://hdl.handle.net/11104/0343342" target="_blank" >https://hdl.handle.net/11104/0343342</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1021/acs.analchem.2c05692" target="_blank" >10.1021/acs.analchem.2c05692</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Determining the Functional Oligomeric State of Membrane- Associated Protein Oligomers Forming Membrane Pores on Giant Lipid Vesicles

  • Original language description

    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.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10403 - Physical chemistry

Result continuities

  • Project

    <a href="/en/project/GC20-01401J" target="_blank" >GC20-01401J: Exploring the structure function relationship of membrane-pore-forming FGF2 oligomers - a single molecule approach</a><br>

  • 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

  • Name of the periodical

    Analytical Chemistry

  • ISSN

    0003-2700

  • e-ISSN

    1520-6882

  • Volume of the periodical

    95

  • Issue of the periodical within the volume

    23

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    9

  • Pages from-to

    8807-8815

  • UT code for WoS article

    000985563200001

  • EID of the result in the Scopus database

    2-s2.0-85159619887