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.
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Chemical Communications, v. 53, n. 53, p. 7337-7340, 2017.
