Interactions of the complete cellobiohydrolase I from Trichodera reesei with microcrystalline cellulose Iβ

Linghao Zhong, James F. Matthews, Michael F. Crowley, Tauna Rignall, César Talón, Joseph M. Cleary, Ross C. Walker, Giridhar Chukkapalli, Clare McCabe, Mark R. Nimlos, Charles L. Brooks, Michael E. Himmel, John W. Brady

Research output: Contribution to journalArticle

40 Citations (Scopus)

Abstract

We describe the construction of a model complex of the cellobiohydrolase I (CBH I) cellulase from Trichoderma reesei bound to a cellulose microfibril in an aqueous environment for use in molecular dynamics (MD) simulations. Preliminary characterization from the initial phases of an MD simulation of this complex is also described. The linker sequence between the two globular domains was found to be quite flexible, and the oligosaccharides bound to this linker were found to prefer to be splayed like the spokes in a wheel due to their hydration requirements. The overall conformations of the two globular domains remained stable in the simulations, although both underwent changes in their orientations.

Original languageEnglish (US)
Pages (from-to)261-273
Number of pages13
JournalCellulose
Volume15
Issue number2
DOIs
StatePublished - Apr 1 2008

Fingerprint

Cellulose 1,4-beta-Cellobiosidase
Molecular dynamics
Cellulose
Oligosaccharides
Cellulase
Computer simulation
Hydration
Conformations
Wheels
microcrystalline cellulose

All Science Journal Classification (ASJC) codes

  • Polymers and Plastics

Cite this

Zhong, L., Matthews, J. F., Crowley, M. F., Rignall, T., Talón, C., Cleary, J. M., ... Brady, J. W. (2008). Interactions of the complete cellobiohydrolase I from Trichodera reesei with microcrystalline cellulose Iβ. Cellulose, 15(2), 261-273. https://doi.org/10.1007/s10570-007-9186-0
Zhong, Linghao ; Matthews, James F. ; Crowley, Michael F. ; Rignall, Tauna ; Talón, César ; Cleary, Joseph M. ; Walker, Ross C. ; Chukkapalli, Giridhar ; McCabe, Clare ; Nimlos, Mark R. ; Brooks, Charles L. ; Himmel, Michael E. ; Brady, John W. / Interactions of the complete cellobiohydrolase I from Trichodera reesei with microcrystalline cellulose Iβ. In: Cellulose. 2008 ; Vol. 15, No. 2. pp. 261-273.
@article{5057d66e4c4c4512812539c629c670a6,
title = "Interactions of the complete cellobiohydrolase I from Trichodera reesei with microcrystalline cellulose Iβ",
abstract = "We describe the construction of a model complex of the cellobiohydrolase I (CBH I) cellulase from Trichoderma reesei bound to a cellulose microfibril in an aqueous environment for use in molecular dynamics (MD) simulations. Preliminary characterization from the initial phases of an MD simulation of this complex is also described. The linker sequence between the two globular domains was found to be quite flexible, and the oligosaccharides bound to this linker were found to prefer to be splayed like the spokes in a wheel due to their hydration requirements. The overall conformations of the two globular domains remained stable in the simulations, although both underwent changes in their orientations.",
author = "Linghao Zhong and Matthews, {James F.} and Crowley, {Michael F.} and Tauna Rignall and C{\'e}sar Tal{\'o}n and Cleary, {Joseph M.} and Walker, {Ross C.} and Giridhar Chukkapalli and Clare McCabe and Nimlos, {Mark R.} and Brooks, {Charles L.} and Himmel, {Michael E.} and Brady, {John W.}",
year = "2008",
month = "4",
day = "1",
doi = "10.1007/s10570-007-9186-0",
language = "English (US)",
volume = "15",
pages = "261--273",
journal = "Cellulose",
issn = "0969-0239",
publisher = "Springer Netherlands",
number = "2",

}

Zhong, L, Matthews, JF, Crowley, MF, Rignall, T, Talón, C, Cleary, JM, Walker, RC, Chukkapalli, G, McCabe, C, Nimlos, MR, Brooks, CL, Himmel, ME & Brady, JW 2008, 'Interactions of the complete cellobiohydrolase I from Trichodera reesei with microcrystalline cellulose Iβ', Cellulose, vol. 15, no. 2, pp. 261-273. https://doi.org/10.1007/s10570-007-9186-0

Interactions of the complete cellobiohydrolase I from Trichodera reesei with microcrystalline cellulose Iβ. / Zhong, Linghao; Matthews, James F.; Crowley, Michael F.; Rignall, Tauna; Talón, César; Cleary, Joseph M.; Walker, Ross C.; Chukkapalli, Giridhar; McCabe, Clare; Nimlos, Mark R.; Brooks, Charles L.; Himmel, Michael E.; Brady, John W.

In: Cellulose, Vol. 15, No. 2, 01.04.2008, p. 261-273.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Interactions of the complete cellobiohydrolase I from Trichodera reesei with microcrystalline cellulose Iβ

AU - Zhong, Linghao

AU - Matthews, James F.

AU - Crowley, Michael F.

AU - Rignall, Tauna

AU - Talón, César

AU - Cleary, Joseph M.

AU - Walker, Ross C.

AU - Chukkapalli, Giridhar

AU - McCabe, Clare

AU - Nimlos, Mark R.

AU - Brooks, Charles L.

AU - Himmel, Michael E.

AU - Brady, John W.

PY - 2008/4/1

Y1 - 2008/4/1

N2 - We describe the construction of a model complex of the cellobiohydrolase I (CBH I) cellulase from Trichoderma reesei bound to a cellulose microfibril in an aqueous environment for use in molecular dynamics (MD) simulations. Preliminary characterization from the initial phases of an MD simulation of this complex is also described. The linker sequence between the two globular domains was found to be quite flexible, and the oligosaccharides bound to this linker were found to prefer to be splayed like the spokes in a wheel due to their hydration requirements. The overall conformations of the two globular domains remained stable in the simulations, although both underwent changes in their orientations.

AB - We describe the construction of a model complex of the cellobiohydrolase I (CBH I) cellulase from Trichoderma reesei bound to a cellulose microfibril in an aqueous environment for use in molecular dynamics (MD) simulations. Preliminary characterization from the initial phases of an MD simulation of this complex is also described. The linker sequence between the two globular domains was found to be quite flexible, and the oligosaccharides bound to this linker were found to prefer to be splayed like the spokes in a wheel due to their hydration requirements. The overall conformations of the two globular domains remained stable in the simulations, although both underwent changes in their orientations.

UR - http://www.scopus.com/inward/record.url?scp=39849101648&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=39849101648&partnerID=8YFLogxK

U2 - 10.1007/s10570-007-9186-0

DO - 10.1007/s10570-007-9186-0

M3 - Article

AN - SCOPUS:39849101648

VL - 15

SP - 261

EP - 273

JO - Cellulose

JF - Cellulose

SN - 0969-0239

IS - 2

ER -