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Fig 1.

Structure of p53 binding domain of MDM2 (A) Ribbon, (B) Surface.

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Fig 1 Expand

Fig 2.

Structure of polyphenols.

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Fig 2 Expand

Fig 3.

(A) backbone RMSD of MDM2 (Red-apigenin, Green- fisetin, Blue-galangin, Purple-luteolin), (B) RMSF profile of MDM2 (Red-apigenin, Green- fisetin, Blue-galangin, Purple-luteolin).

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Fig 3 Expand

Fig 4.

(A) Radius of gyration profile of MDM2 (Red-apigenin, Green- fisetin, Blue-galangin, Purple-luteolin)., (B) SASA profile of MDM2 (Red-apigenin, Green- fisetin, Blue-galangin, Purple-luteolin).

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Fig 4 Expand

Fig 5.

Apigenin-MDM2 complex at 15 ns (A) cartoon representation, (B) surface structure.

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Fig 5 Expand

Fig 6.

Fisetin-MDM2 complex at 15 ns (A) cartoon representation, (B) surface structure.

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Fig 6 Expand

Fig 7.

Galangin-MDM2 complex at 15 ns (A) cartoon representation, (B) surface structure.

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Fig 7 Expand

Fig 8.

Luteolin-MDM2 complex at 15 ns (A) cartoon representation, (B) surface structure.

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Fig 8 Expand

Fig 9.

Polyphenol-MDM2 interaction plot generated by Ligplot (A) Apigenin, (B) Fisetin, (C) Galangin, (D) Luteolin.

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Fig 9 Expand

Table 1.

Average MM/PBSA free energies of MDM2-polyphenol complexes calculated from the MD simulations performed in triplicate.

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Table 1 Expand

Fig 10.

Penetration of polyphenol in hydrophobic groove of MDM2.

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Fig 10 Expand

Fig 11.

Covariance matrix of MDM2 during 15 ns MD simulation (Upper left-Apigenin, Upper right-Fisetin, Lower left-Galangin, Lower right-Luteolin).

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Fig 11 Expand

Table 2.

Dominant motions of atom in helix2, helix 4 and loop.

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Table 2 Expand