Molecular simulation evidence for processive motion of Trichoderma reesei Cel7A during cellulose depolymerization

Xiongce Zhao, Tauna R. Rignall, Clare McCabe*, William S. Adney, Michael E. Himmel

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

29 Citations (Scopus)

Abstract

We present free energy calculations for the Trichoderma reesei Cel7A (cellobiohydrolase I) linker peptide from molecular dynamics simulations directed towards understanding the linker role in cellulose hydrolysis. The calculations predict an energy storage mechanism of the linker under stretching/compression that is consistent with processive depolymerization. The linker exhibits two stable states at lengths of 2.5 nm and 5.5 nm during extension/compression, with a free energy difference of 10.5 kcal/mol between the two states separated by an energy barrier. The switching between stable states supports the hypothesis that the linker peptide has the capacity to store energy in a manner similar to a spring.

Original languageEnglish
Pages (from-to)284-288
Number of pages5
JournalChemical Physics Letters
Volume460
Issue number1-3
DOIs
Publication statusPublished - 20 Jul 2008

ASJC Scopus subject areas

  • Physics and Astronomy(all)
  • Physical and Theoretical Chemistry

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