| dc.contributor.author | Bernardino, K. | |
| dc.contributor.author | Pinto, M. E.F. [UNESP] | |
| dc.contributor.author | Bolzani, V. S. [UNESP] | |
| dc.contributor.author | De Moura, A. F. | |
| dc.contributor.author | Batista, J. M. | |
| dc.date.accessioned | 2018-12-11T16:47:58Z | |
| dc.date.available | 2018-12-11T16:47:58Z | |
| dc.date.issued | 2017-01-01 | |
| dc.identifier | http://dx.doi.org/10.1039/c7cc02333b | |
| dc.identifier.citation | Chemical Communications, v. 53, n. 53, p. 7337-7340, 2017. | |
| dc.identifier.issn | 1364-548X | |
| dc.identifier.issn | 1359-7345 | |
| dc.identifier.uri | http://hdl.handle.net/11449/169874 | |
| dc.description.abstract | A 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.extent | 7337-7340 | |
| dc.language.iso | eng | |
| dc.relation.ispartof | Chemical Communications | |
| dc.source | Scopus | |
| dc.title | Pinpointing disulfide connectivities in cysteine-rich proteins | en |
| dc.type | Artigo | |
| dc.contributor.institution | Universidade Federal de São Carlos (UFSCar) | |
| dc.contributor.institution | Universidade Estadual Paulista (UNESP) | |
| dc.description.affiliation | Department of Chemistry Federal University of São Carlos-UFSCarZ | |
| dc.description.affiliation | Institute of Chemistry São Paulo State University-UNESP | |
| dc.description.affiliationUnesp | Institute of Chemistry São Paulo State University-UNESP | |
| dc.identifier.doi | 10.1039/c7cc02333b | |
| dc.rights.accessRights | Acesso restrito | |
| dc.identifier.scopus | 2-s2.0-85021626553 | |
| dc.relation.ispartofsjr | 2,555 | |
