Influence of protein crowder size on hydration structure and dynamics in macromolecular crowding

Po hung Wang, Isseki Yu, Michael Feig, Yuji Sugita

    Research output: Contribution to journalArticle

    • 1 Citations

    Abstract

    We investigate the effects of protein crowder sizes on hydration structure and dynamics in macromolecular crowded systems by all-atom MD simulations. The crowded systems consisting of only small proteins showed larger total surface areas than those of large proteins at the same volume fractions. As a result, more water molecules were trapped within the hydration shells, slowing down water diffusion. The simulation results suggest that the protein crowder size is another factor to determine the effect of macromolecular crowding and to explain the experimental kinetic data of proteins and DNAs in the presence of crowding agents.

    Original languageEnglish (US)
    Pages (from-to)63-70
    Number of pages8
    JournalChemical Physics Letters
    Volume671
    DOIs
    StatePublished - Mar 1 2017

    Profile

    proteins
    crowding
    hydration
    Hydration
    water
    simulation
    Spontaneous Fractures
    deoxyribonucleic acid
    kinetics
    atoms
    molecules
    Edema Disease of Swine
    Inborn Errors Amino Acid Metabolism
    Feline Sarcoma Viruses
    Iduronidase
    Atoms
    Molecules
    Kinetics

    Keywords

    • Diffusion coefficient
    • Hydration
    • Macromolecular crowding
    • Protein crowders
    • Solvent accessible surface area

    ASJC Scopus subject areas

    • Physics and Astronomy(all)
    • Physical and Theoretical Chemistry

    Cite this

    Influence of protein crowder size on hydration structure and dynamics in macromolecular crowding. / Wang, Po hung; Yu, Isseki; Feig, Michael; Sugita, Yuji.

    In: Chemical Physics Letters, Vol. 671, 01.03.2017, p. 63-70.

    Research output: Contribution to journalArticle

    Wang, Po hung; Yu, Isseki; Feig, Michael; Sugita, Yuji / Influence of protein crowder size on hydration structure and dynamics in macromolecular crowding.

    In: Chemical Physics Letters, Vol. 671, 01.03.2017, p. 63-70.

    Research output: Contribution to journalArticle

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