Number of the records: 1  

Optimized OPEP Force Field for Simulation of Crowded Protein Solutions

  1. 1.
    SYSNO ASEP0571064
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JČlánek ve WOS
    TitleOptimized OPEP Force Field for Simulation of Crowded Protein Solutions
    Author(s) Timr, Štěpán (UFCH-W)
    Melchionna, S. (IT)
    Derreumaux, P. (FR)
    Sterpone, F. (FR)
    Source TitleJournal of Physical Chemistry B. - : American Chemical Society - ISSN 1520-6106
    Roč. 127, č. 16 (2023), s. 3616-3623
    Number of pages8 s.
    Languageeng - English
    CountryUS - United States
    KeywordsOptimized Potential for Efficient Protein ; diffusion ; molecular mechanics
    Subject RIVCF - Physical ; Theoretical Chemistry
    OECD categoryPhysical chemistry
    Method of publishingOpen access
    Institutional supportUFCH-W - RVO:61388955
    UT WOS000975438500001
    EID SCOPUS85153989015
    DOI10.1021/acs.jpcb.3c00253
    AnnotationMacromolecular crowding has profound effects on the mobility of proteins, with strong implications on the rates of intracellular processes. To describe the dynamics of crowded environments, detailed molecular models are needed, capturing the structures and interactions arising in the crowded system. In this work, we present OPEPv7, which is a coarse-grained force field at amino-acid resolution, suited for rigid-body simulations of the structure and dynamics of crowded solutions formed by globular proteins. Using the OPEP protein model as a starting point, we have refined the intermolecular interactions to match the experimentally observed dynamical slowdown caused by crowding. The resulting force field successfully reproduces the diffusion slowdown in homogeneous and heterogeneous protein solutions at different crowding conditions. Coupled with the lattice Boltzmann technique, it allows the study of dynamical phenomena in protein assemblies and opens the way for the in silico rheology of protein solutions.
    WorkplaceJ. Heyrovsky Institute of Physical Chemistry
    ContactMichaela Knapová, michaela.knapova@jh-inst.cas.cz, Tel.: 266 053 196
    Year of Publishing2024
    Electronic addresshttps://hdl.handle.net/11104/0342374
Number of the records: 1  

  This site uses cookies to make them easier to browse. Learn more about how we use cookies.