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Pinpointing disulfide connectivities in cysteine-rich proteins

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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.

Graphical abstract: Pinpointing disulfide connectivities in cysteine-rich proteins

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Publication details

The article was received on 27 Mar 2017, accepted on 05 May 2017 and first published on 05 May 2017


Article type: Communication
DOI: 10.1039/C7CC02333B
Citation: Chem. Commun., 2017, Advance Article
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    Pinpointing disulfide connectivities in cysteine-rich proteins

    K. Bernardino, M. E. F. Pinto, V. S. Bolzani, A. F. de Moura and J. M. Batista Junior, Chem. Commun., 2017, Advance Article , DOI: 10.1039/C7CC02333B

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