Pinpointing disulfide connectivities in cysteine-rich proteins

dc.contributorUniversidade Federal de São Carlos (UFSCar)
dc.contributorUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2018-12-11T16:47:58Z
dc.date.available2018-12-11T16:47:58Z
dc.date.created2018-12-11T16:47:58Z
dc.date.issued2017-01-01
dc.identifierChemical Communications, v. 53, n. 53, p. 7337-7340, 2017.
dc.identifier1364-548X
dc.identifier1359-7345
dc.identifierhttp://hdl.handle.net/11449/169874
dc.identifier10.1039/c7cc02333b
dc.identifier2-s2.0-85021626553
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.
dc.languageeng
dc.relationChemical Communications
dc.relation2,555
dc.rightsAcesso restrito
dc.sourceScopus
dc.titlePinpointing disulfide connectivities in cysteine-rich proteins
dc.typeArtículos de revistas


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