Pinpointing disulfide connectivities in cysteine-rich proteinsElectronic supplementary information (ESI) available: Experimental section and theoretical calculations. See DOI: 10.1039/c7cc02333b

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 c...

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Bibliographic Details
Main Authors: Bernardino, K, Pinto, M. E. F, Bolzani, V. S, de Moura, A. F, Batista Junior, J. M
Format: Article
Language:English
Online Access:Get full text
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Summary: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. The sequence and order of disulfide bond formation in cysteine-rich proteins, and the resulting conformational changes, are assessed via a thermodynamic perturbation protocol.
ISSN:1359-7345
1364-548X
DOI:10.1039/c7cc02333b