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Issue 53, 2017
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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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Article information


Submitted
27 Mar 2017
Accepted
05 May 2017
First published
05 May 2017

Chem. Commun., 2017,53, 7337-7340
Article type
Communication

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, 53, 7337
DOI: 10.1039/C7CC02333B

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