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 proceedingConference abstract in proceedingsScientific

    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 languageEnglish
    Title of host publicationAdvances in biomolecular simulations
    EditorsHelena L. Chum
    PublisherAmerican Chemical Society ACS
    DOIs
    Publication statusPublished - 1991
    MoE publication typeNot Eligible
    EventCellulose '91 - New Orleans, United States
    Duration: 2 Dec 19916 Dec 1991

    Publication series

    SeriesAIP Conference Proceedings
    Number1
    Volume239
    ISSN0094-243X

    Conference

    ConferenceCellulose '91
    Country/TerritoryUnited States
    CityNew Orleans
    Period2/12/916/12/91

    Keywords

    • molecular modelling
    • chemical modelling

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