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

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Cellulose 1,4-beta-Cellobiosidase
Molecular modeling
cellulose
Cellulose
Crystalline materials
interactions
polysaccharides
algae
Algae
Polysaccharides
Molecular dynamics
enzymes
Crystal structure
Vacuum
molecular dynamics
vacuum
crystal structure
Substrates
Enzymes

Keywords

  • molecular modelling
  • chemical modelling

Cite this

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title = "Interaction studies of the tail domain of cellobiohydrolase I and crystalline cellulose using molecular modelling",
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.",
keywords = "molecular modelling, chemical modelling",
author = "Lauri Kuutti and Leif Laaksonen and Tuula Teeri",
note = "Project code: BIO1003",
year = "1991",
doi = "10.1051/jcp/1991882663",
language = "English",
volume = "88",
pages = "2663 -- 2667",
journal = "ChemPhysChem",
issn = "1439-4235",
publisher = "Wiley-VCH Verlag",

}

Interaction studies of the tail domain of cellobiohydrolase I and crystalline cellulose using molecular modelling. / Kuutti, Lauri; Laaksonen, Leif; Teeri, Tuula.

In: Journal de Chimie Physique et de Physico-Chimie Biologique, Vol. 88, 1991, p. 2663 - 2667.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Interaction studies of the tail domain of cellobiohydrolase I and crystalline cellulose using molecular modelling

AU - Kuutti, Lauri

AU - Laaksonen, Leif

AU - Teeri, Tuula

N1 - Project code: BIO1003

PY - 1991

Y1 - 1991

N2 - 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.

AB - 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.

KW - molecular modelling

KW - chemical modelling

U2 - 10.1051/jcp/1991882663

DO - 10.1051/jcp/1991882663

M3 - Article

VL - 88

SP - 2663

EP - 2667

JO - ChemPhysChem

JF - ChemPhysChem

SN - 1439-4235

ER -