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
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Czech description
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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