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 abstract in proceedings › Scientific

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	Cellulose '91
Editors	Helena L. Chum
Publisher	American Chemical Society ACS
DOIs	https://doi.org/10.1063/1.41322
Publication status	Published - 1991
MoE publication type	Not Eligible
Event	Cellulose '91 - New Orleans, United States Duration: 2 Dec 1991 → 6 Dec 1991

Conference

Conference	Cellulose '91
Country	United States
City	New Orleans
Period	2/12/91 → 6/12/91

Keywords

molecular modelling
chemical modelling

Access to Document

10.1063/1.41322

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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 Abstract no. 28; Cellulose '91 ; Conference date: 02-12-1991 Through 06-12-1991",

year = "1991",

doi = "10.1063/1.41322",

language = "English",

editor = "Chum, {Helena L.}",

booktitle = "Cellulose '91",

publisher = "American Chemical Society ACS",

address = "United States",

}

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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 Abstract no. 28

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 abstract in proceedings

BT - Cellulose '91

A2 - Chum, Helena L.

PB - American Chemical Society ACS

T2 - Cellulose '91

Y2 - 2 December 1991 through 6 December 1991

ER -