论文部分内容阅读
A series of theoretical approaches,including conventional FF03 and FF03-based polarization model,as well as the generalized energy-based fragmentation(GEBF) quantum chemistry method,have been applied to investigate the interactions between acetate ion(CH3COO-) and the α-subunit of human adult hemoglobin(designated as Hb-α) at four binding sites(Lys16,Lys90,Arg92,and Lys127),respectively.The FF03-based polarizable force fields show that the interaction energies between the CH3COO-group and Hb-α follow the trend of Arg92>Lys127>Lys90>Lys16.The complexation of CH3COO-with Hb-α is governed by the long-range electrostatic interactions and steric effect.
A series of theoretical approaches, including conventional FF03 and FF03-based polarization models, as well as the generalized energy-based fragmentation (GEBF) quantum chemistry method, have been applied to investigate the interactions between acetate ion (CH3COO-) and the α- subunit of human adult hemoglobin (designated as Hb-α) at four binding sites (Lys16, Lys90, Arg92, and Lys127), respectively. The FF03-based polarizable force fields show that the interaction energies between the CH3COO-group and Hb-α follow the trend of Arg92> Lys127> Lys90> Lys16. The complexation of CH3COO-with Hb-alpha is governed by the long-range electrostatic interactions and steric effect.