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Polyethylene glycol perturbs the unfolding of CRABP I: A correlation between experimental and theoretical approach

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F21%3A00121266" target="_blank" >RIV/00216224:14740/21:00121266 - isvavai.cz</a>

  • Result on the web

    <a href="https://doi.org/10.1016/j.colsurfb.2021.111696" target="_blank" >https://doi.org/10.1016/j.colsurfb.2021.111696</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.colsurfb.2021.111696" target="_blank" >10.1016/j.colsurfb.2021.111696</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Polyethylene glycol perturbs the unfolding of CRABP I: A correlation between experimental and theoretical approach

  • Original language description

    The importance of macromolecules paves the way towards a detailed molecular level investigation as all most all cellular processes occurring at the interior of cells in the form of proteins, enzymes, and other biological molecules are significantly affected because of their crowding. Thus, exploring the role of crowding environment on the denaturation and renaturation kinetics of protein molecules is of great importance. Here, we have employed CRABP I (cellular retinoic acid binding protein I), as a model protein along with different molecular weights of Polyethylene glycol (PEG) as molecular crowders. The experimental evaluations were done by accessing the protein secondary structure analysis using circular dichroism (CD) spectroscopy and unfolding kinetics using intrinsic fluorescence of CRABP I at 37 °C to mimic the in vivo crowding environment. The unfolding kinetics results indicated that both PEG 2000 and PEG 4000 act as stabilizers by retarding the unfolding kinetic rates. Both kinetic and stability outcomes presented the importance of crowding environment on stability and kinetics of CRABP I. The molecular dynamics (MD) studies revealed that thirteen PEG 2000 molecules assembled during the 500 ns simulation, which increases the stability and percentage of β-sheet. The experimental findings were well supported by the molecular dynamics simulation results.

  • 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

    10608 - Biochemistry and molecular biology

Result continuities

  • Project

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

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2021

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Colloids and Surfaces B: Biointerfaces

  • ISSN

    0927-7765

  • e-ISSN

    1873-4367

  • Volume of the periodical

    202

  • Issue of the periodical within the volume

    June

  • Country of publishing house

    NL - THE KINGDOM OF THE NETHERLANDS

  • Number of pages

    10

  • Pages from-to

    111696

  • UT code for WoS article

    000663336700004

  • EID of the result in the Scopus database

    2-s2.0-85103327693