We report the systematic survey of the binding free energies at the interface between a carbohydrate binding module(CBM)of Cel7A and the celluloseⅢ_(1)crystal model using grid docking searches and molecular dynamics ...We report the systematic survey of the binding free energies at the interface between a carbohydrate binding module(CBM)of Cel7A and the celluloseⅢ_(1)crystal model using grid docking searches and molecular dynamics simulations.The two hydrophobic crystal surfaces were involved in the distinct energy minima of the binding free energy.The complex models,each with the CBM at the minimum energy position,stably formed in the solution state.The binding free energies of the celluloseⅢ_(1)complex models,based on both static and dynamics states,were comparable to those of the native cellulose complex models.However,the celluloseⅢ_(1)crystal had a larger binding surface,which is compatible with the observed high enzymatic activity of Cel7A for the celluloseⅢ_(1)substrate.展开更多
基金supported by JSPS KAKENHI Grant Number 17K00409。
文摘We report the systematic survey of the binding free energies at the interface between a carbohydrate binding module(CBM)of Cel7A and the celluloseⅢ_(1)crystal model using grid docking searches and molecular dynamics simulations.The two hydrophobic crystal surfaces were involved in the distinct energy minima of the binding free energy.The complex models,each with the CBM at the minimum energy position,stably formed in the solution state.The binding free energies of the celluloseⅢ_(1)complex models,based on both static and dynamics states,were comparable to those of the native cellulose complex models.However,the celluloseⅢ_(1)crystal had a larger binding surface,which is compatible with the observed high enzymatic activity of Cel7A for the celluloseⅢ_(1)substrate.
