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

Lauri Kuutti, Leif Laaksonen, Tuula Teeri

Research output: Contribution to journalArticleScientificpeer-review

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.

Original languageEnglish
Pages (from-to)2663 - 2667
Number of pages5
JournalJournal de Chimie Physique et de Physico-Chimie Biologique
Volume88
DOIs
Publication statusPublished - 1991
MoE publication typeA1 Journal article-refereed

Keywords

  • molecular modelling
  • chemical modelling

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