Selected article for: "hydrophobic interaction and Pi alkyl"

Author: Parvez, Mohammad K.; Tabish Rehman, Md.; Alam, Perwez; Al-Dosari, Mohammed S.; Alqasoumi, Saleh I.; Alajmi, Mohammed F.
Title: Plant-derived antiviral drugs as novel hepatitis B virus inhibitors: Cell culture and molecular docking study
  • Document date: 2018_12_26
  • ID: xibqsjib_59
    Snippet: Embelin (Fig. 1J ) interacted with HBV Pol by forming three hydrogen bonds with Lys32 and His160. It also formed one alkyl hydrophobic interaction with Pro5 and three Pi-alkyl hydrophobic interactions with Trp3, Arg41 and Ala86 (Fig. 7J ). Other residues that surrounded embelin were Glu1, Asp2, Gly4, Gln39, Ser40, Leu42, Ser85 and Ala87. The Gibb's free energy of embelin-Pol interaction was predicted to be À6.1 kcal/mol which corresponded to a b.....
    Document: Embelin (Fig. 1J ) interacted with HBV Pol by forming three hydrogen bonds with Lys32 and His160. It also formed one alkyl hydrophobic interaction with Pro5 and three Pi-alkyl hydrophobic interactions with Trp3, Arg41 and Ala86 (Fig. 7J ). Other residues that surrounded embelin were Glu1, Asp2, Gly4, Gln39, Ser40, Leu42, Ser85 and Ala87. The Gibb's free energy of embelin-Pol interaction was predicted to be À6.1 kcal/mol which corresponded to a binding constant of 2.4 Â 10 4 /mol (Table 2) .

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