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dc.contributor.authorBernardino, K.
dc.contributor.authorPinto, M. E.F. [UNESP]
dc.contributor.authorBolzani, V. S. [UNESP]
dc.contributor.authorDe Moura, A. F.
dc.contributor.authorBatista, J. M.
dc.date.accessioned2018-12-11T16:47:58Z
dc.date.available2018-12-11T16:47:58Z
dc.date.issued2017-01-01
dc.identifierhttp://dx.doi.org/10.1039/c7cc02333b
dc.identifier.citationChemical Communications, v. 53, n. 53, p. 7337-7340, 2017.
dc.identifier.issn1364-548X
dc.identifier.issn1359-7345
dc.identifier.urihttp://hdl.handle.net/11449/169874
dc.description.abstractA simple MD-based protocol is presented to accurately predict both the sequence and order of disulfide bond formation in proteins containing multiple cysteine residues. It provides a detailed description of their dynamical and structural features, which can be used to perform ensemble-Averaged ECD calculations. Plant cyclotides are used as model compounds.en
dc.format.extent7337-7340
dc.language.isoeng
dc.relation.ispartofChemical Communications
dc.sourceScopus
dc.titlePinpointing disulfide connectivities in cysteine-rich proteinsen
dc.typeArtigo
dc.contributor.institutionUniversidade Federal de São Carlos (UFSCar)
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)
dc.description.affiliationDepartment of Chemistry Federal University of São Carlos-UFSCarZ
dc.description.affiliationInstitute of Chemistry São Paulo State University-UNESP
dc.description.affiliationUnespInstitute of Chemistry São Paulo State University-UNESP
dc.identifier.doi10.1039/c7cc02333b
dc.rights.accessRightsAcesso restrito
dc.identifier.scopus2-s2.0-85021626553
dc.relation.ispartofsjr2,555
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