Issue 53, 2017

Pinpointing disulfide connectivities in cysteine-rich proteins

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

Supplementary files

Article information

Article type
Communication
Submitted
27 mar. 2017
Accepted
05 may. 2017
First published
05 may. 2017

Chem. Commun., 2017,53, 7337-7340

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

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements