Interaction studies of the tail domain of cellobiohydrolase I and crystalline cellulose using molecular modelling

VTT, Biotechnical Laboratory, PO Box 202, SF-02151 Espoo, Finland.

Abstract

A surface model of crystalline cellulose was constructed based on the crystal structure of the sea alga Valonia ventricosa (Gardner and Blackwell, 1974). The structure of the crystalline cellulose was optimized by minimizing the intra- and intermolecular energies. Interactions between the optimized crystalline cellulose and the tail domain of CBH I were explored using molecular dynamics calculations carried out in vacuum. The binding of the tail domain to a relatively large portion of a linear polysaccharide has shown to involve numerous individually weak interactions (van der Waals and H-bonds). This preliminary research is related to the use of molecular modelling in a study to explain the weak interactions involved in the enzyme-cellulose substrate complex.