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

Lauri Kuutti; Leif Laaksonen; Tuula Teeri

doi:10.1063/1.41322

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

Lauri Kuutti, Leif Laaksonen, Tuula Teeri

Research output: Chapter in Book/Report/Conference proceeding › Conference article in proceedings › Scientific › peer-review

Abstract

Cellulose is the most abundant organic compound in the biosphere. In nature, crystalline cellulose is hydrolysed by specific enzymes called cellulases. Understanding the physico‐chemical nature of these enzymatic processes will be essential for developing new energy saving and non polluting methods for cellulose degradation and modification.

Original language	English
Title of host publication	Advances in biomolecular simulations
Place of Publication	Obernai
DOIs	https://doi.org/10.1063/1.41322
Publication status	Published - 1991
MoE publication type	A4 Article in a conference publication
Event	International Symposium on Advances in Biomolecular Simulations - Obernai, France Duration: 12 Mar 1991 → 14 Mar 1991

Publication series

Series	AIP Conference Proceedings
Volume	239
ISSN	0094-243X

Conference

Conference	International Symposium on Advances in Biomolecular Simulations
Country/Territory	France
City	Obernai
Period	12/03/91 → 14/03/91

Keywords

molecular modelling
chemical modelling

Access to Document

10.1063/1.41322

Cite this

@inproceedings{1ecb93b4b66b45f0a8f3da6e2a8b971e,

title = "Interaction studies of the tail domain of cellobiohydrolase I and crystalline cellulose using molecular modelling",

abstract = "Cellulose is the most abundant organic compound in the biosphere. In nature, crystalline cellulose is hydrolysed by specific enzymes called cellulases. Understanding the physico‐chemical nature of these enzymatic processes will be essential for developing new energy saving and non polluting methods for cellulose degradation and modification.",

keywords = "molecular modelling, chemical modelling",

author = "Lauri Kuutti and Leif Laaksonen and Tuula Teeri",

note = "Project code: BIO1003; International Symposium on Advances in Biomolecular Simulations ; Conference date: 12-03-1991 Through 14-03-1991",

year = "1991",

doi = "10.1063/1.41322",

language = "English",

series = "AIP Conference Proceedings",

publisher = "American Institute of Physics (AIP)",

booktitle = "Advances in biomolecular simulations",

}

Kuutti, L, Laaksonen, L & Teeri, T 1991, Interaction studies of the tail domain of cellobiohydrolase I and crystalline cellulose using molecular modelling. in Advances in biomolecular simulations., 27, Obernai, AIP Conference Proceedings, vol. 239, International Symposium on Advances in Biomolecular Simulations, Obernai, France, 12/03/91. https://doi.org/10.1063/1.41322

Interaction studies of the tail domain of cellobiohydrolase I and crystalline cellulose using molecular modelling. / Kuutti, Lauri; Laaksonen, Leif; Teeri, Tuula.
Advances in biomolecular simulations. Obernai, 1991. 27 (AIP Conference Proceedings, Vol. 239).

Research output: Chapter in Book/Report/Conference proceeding › Conference article in proceedings › Scientific › peer-review

TY - GEN

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 - Cellulose is the most abundant organic compound in the biosphere. In nature, crystalline cellulose is hydrolysed by specific enzymes called cellulases. Understanding the physico‐chemical nature of these enzymatic processes will be essential for developing new energy saving and non polluting methods for cellulose degradation and modification.

AB - Cellulose is the most abundant organic compound in the biosphere. In nature, crystalline cellulose is hydrolysed by specific enzymes called cellulases. Understanding the physico‐chemical nature of these enzymatic processes will be essential for developing new energy saving and non polluting methods for cellulose degradation and modification.

KW - molecular modelling

KW - chemical modelling

U2 - 10.1063/1.41322

DO - 10.1063/1.41322

M3 - Conference article in proceedings

T3 - AIP Conference Proceedings

BT - Advances in biomolecular simulations

CY - Obernai

T2 - International Symposium on Advances in Biomolecular Simulations

Y2 - 12 March 1991 through 14 March 1991

ER -

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

Abstract

Publication series

Conference

Keywords

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Cite this