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molecular dynamics rmsd changes  (Molecular Dynamics Inc)

 
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    Molecular Dynamics Inc molecular dynamics rmsd changes
    A <t>:</t> <t>Molecular</t> dynamics <t>RMSD</t> changes of the complex of luteolin and PPAR-γ within 100 ns; B : The RMSF position of the complex of luteolin and PPAR-γ; C : Protein Ligand contacts of the complex of luteolin and PPAR-γ, where green represents hydrogen bonds, purple represents hydrophobic bonds, and blue represents water bridges; D : Timeline representation of the interactions and contacts
    Molecular Dynamics Rmsd Changes, supplied by Molecular Dynamics Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/molecular+dynamics+rmsd+changes/changes+dynamics+molecular+rmsd/pmc12583437-103-4-4
    Average 86 stars, based on 1 article reviews
    molecular dynamics rmsd changes - by Bioz Stars, 2026-10
    86/100 stars

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    1) Product Images from "Traditional processing unlocks anti-atherogenic potential of perilla fruit via PPAR-γ activation by luteolin"

    Article Title: Traditional processing unlocks anti-atherogenic potential of perilla fruit via PPAR-γ activation by luteolin

    Journal: Bioresources and Bioprocessing

    doi: 10.1186/s40643-025-00957-7

    A : Molecular dynamics RMSD changes of the complex of luteolin and PPAR-γ within 100 ns; B : The RMSF position of the complex of luteolin and PPAR-γ; C : Protein Ligand contacts of the complex of luteolin and PPAR-γ, where green represents hydrogen bonds, purple represents hydrophobic bonds, and blue represents water bridges; D : Timeline representation of the interactions and contacts
    Figure Legend Snippet: A : Molecular dynamics RMSD changes of the complex of luteolin and PPAR-γ within 100 ns; B : The RMSF position of the complex of luteolin and PPAR-γ; C : Protein Ligand contacts of the complex of luteolin and PPAR-γ, where green represents hydrogen bonds, purple represents hydrophobic bonds, and blue represents water bridges; D : Timeline representation of the interactions and contacts

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    Article Title: Traditional processing unlocks anti-atherogenic potential of perilla fruit via PPAR-γ activation by luteolin.
    Article Snippet: Stir-frying likely accelerates its hydrolysis or oxidation, as phenolic esters like chlorogenic acid are thermally labile-this could Fig. 4 A: Molecular dynamics RMSD changes of the complex of luteolin and PPAR-γ within 100 ns; B: The RMSF position of the complex of luteolin and PPAR-γ; C: Protein Ligand contacts of the complex of luteolin and PPAR-γ, where green represents hydrogen bonds, purple represents hydrophobic bonds, and blue represents water bridges; D: Timeline representation of the interactions and contacts explain the 25% reduction in its content (S1: 1795.04 μg/g vs. S2: 1340.73 μg/g).

    Article Title: Traditional processing unlocks anti-atherogenic potential of perilla fruit via PPAR-γ activation by luteolin
    Article Snippet: Fig. 4 A : Molecular dynamics RMSD changes of the complex of luteolin and PPAR-γ within 100 ns; B : The RMSF position of the complex of luteolin and PPAR-γ; C : Protein Ligand contacts of the complex of luteolin and PPAR-γ, where green represents hydrogen bonds, purple represents hydrophobic bonds, and blue represents water bridges; D : Timeline representation of the interactions and contacts



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    A <t>:</t> <t>Molecular</t> dynamics <t>RMSD</t> changes of the complex of luteolin and PPAR-γ within 100 ns; B : The RMSF position of the complex of luteolin and PPAR-γ; C : Protein Ligand contacts of the complex of luteolin and PPAR-γ, where green represents hydrogen bonds, purple represents hydrophobic bonds, and blue represents water bridges; D : Timeline representation of the interactions and contacts
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    A <t>:</t> <t>Molecular</t> dynamics <t>RMSD</t> changes of the complex of luteolin and PPAR-γ within 100 ns; B : The RMSF position of the complex of luteolin and PPAR-γ; C : Protein Ligand contacts of the complex of luteolin and PPAR-γ, where green represents hydrogen bonds, purple represents hydrophobic bonds, and blue represents water bridges; D : Timeline representation of the interactions and contacts
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    A : Molecular dynamics RMSD changes of the complex of luteolin and PPAR-γ within 100 ns; B : The RMSF position of the complex of luteolin and PPAR-γ; C : Protein Ligand contacts of the complex of luteolin and PPAR-γ, where green represents hydrogen bonds, purple represents hydrophobic bonds, and blue represents water bridges; D : Timeline representation of the interactions and contacts

    Journal: Bioresources and Bioprocessing

    Article Title: Traditional processing unlocks anti-atherogenic potential of perilla fruit via PPAR-γ activation by luteolin

    doi: 10.1186/s40643-025-00957-7

    Figure Lengend Snippet: A : Molecular dynamics RMSD changes of the complex of luteolin and PPAR-γ within 100 ns; B : The RMSF position of the complex of luteolin and PPAR-γ; C : Protein Ligand contacts of the complex of luteolin and PPAR-γ, where green represents hydrogen bonds, purple represents hydrophobic bonds, and blue represents water bridges; D : Timeline representation of the interactions and contacts

    Article Snippet: Fig. 4 A : Molecular dynamics RMSD changes of the complex of luteolin and PPAR-γ within 100 ns; B : The RMSF position of the complex of luteolin and PPAR-γ; C : Protein Ligand contacts of the complex of luteolin and PPAR-γ, where green represents hydrogen bonds, purple represents hydrophobic bonds, and blue represents water bridges; D : Timeline representation of the interactions and contacts

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