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dc.contributor.authorLima, Leonardo H.F.-
dc.contributor.authorSerpa, Viviane I.-
dc.contributor.authorRosseto, Flávio R.-
dc.contributor.authorSartori, Geraldo Rodrigues-
dc.contributor.authorde Oliveira Neto, Mario-
dc.contributor.authorMartínez, Leandro-
dc.contributor.authorPolikarpov, Igor-
dc.identifier.citationCellulose, v. 20, n. 4, p. 1573-1585, 2013.-
dc.description.abstractCellobiohydrolases hydrolyze cellulose releasing cellobiose units. They are very important for a number of biotechnological applications, such as, for example, production of cellulosic ethanol and cotton fiber processing. The Trichoderma cellobiohydrolase I (CBH1 or Cel7A) is an industrially important exocellulase. It exhibits a typical two domain architecture, with a small C-terminal cellulose-binding domain and a large N-terminal catalytic core domain, connected by an O-glycosylated linker peptide. The mechanism by which the linker mediates the concerted action of the two domains remains a conundrum. Here, we probe the protein shape and domain organization of the CBH1 of Trichoderma harzianum (ThCel7A) by small angle X-ray scattering (SAXS) and structural modeling. Our SAXS data shows that ThCel7A linker is partially-extended in solution. Structural modeling suggests that this linker conformation is stabilized by inter- and intra-molecular interactions involving the linker peptide and its O-glycosylations. © 2013 Springer Science+Business Media Dordrecht.en
dc.subjectBiotechnological applications-
dc.subjectCellulose-binding domain-
dc.subjectIntramolecular interactions-
dc.subjectSmall angle X-ray scattering-
dc.subjectTwo-domain architecture-
dc.subjectCellulosic ethanol-
dc.subjectMolecular structure-
dc.subjectX ray scattering-
dc.titleSmall-angle X-ray scattering and structural modeling of full-length: Cellobiohydrolase I from Trichoderma harzianumen
dc.contributor.institutionUniversidade de São Paulo (USP)-
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.contributor.institutionUniversidade Estadual de Campinas (UNICAMP)-
dc.description.affiliationGrupo de Biotecnologia Molecular, Instituto de Física de São Carlos (IFSC) Universidade de São Paulo (USP), Av. Trabalhador São-carlense, 400, Centro, São Carlos, SP, 13566-570-
dc.description.affiliationDepartamento de Física e Biofísica, Instituto de Biociências de Botucatu Unesp, Univ Estadual Paulista, Distrito de Rubião Jr. s/n, Botucatu, SP-
dc.description.affiliationInstitute of Chemistry of São Carlos University of São Paulo, São Carlos, SP-
dc.description.affiliationInstitute of Chemistry State University of Campinas (UNICAMP), Campinas, SP-
dc.description.affiliationUnespDepartamento de Física e Biofísica, Instituto de Biociências de Botucatu Unesp, Univ Estadual Paulista, Distrito de Rubião Jr. s/n, Botucatu, SP-
dc.rights.accessRightsAcesso restrito-
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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