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BioMed Research International
Volume 2013 (2013), Article ID 170586, 14 pages
http://dx.doi.org/10.1155/2013/170586
Research Article

Computational Analysis of the Soluble Form of the Intracellular Chloride Ion Channel Protein CLIC1

1School of Medical and Molecular Biosciences, University of Technology Sydney, P.O. Box 123, Broadway, NSW 2007, Australia
2School of Physics, University of New South Wales, Sydney, NSW 2052, Australia
3St Vincent’s Centre for Applied Medical Research, St Vincent’s Hospital, Darlinghurst, NSW 2010, Australia

Received 10 April 2013; Revised 26 June 2013; Accepted 27 June 2013

Academic Editor: Serdar Kuyucak

Copyright © 2013 Peter M. Jones et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Supplementary Material

Suppl. Table 1 details contributions to the ionisation energy of residue C24 at pH7. There are an additional eight Supplementary Figures, most of which have several panels. These figures describe: the time course of conformational changes during the simulations; the rotation of crucial residues; the prediction of phosphorylation sites; protein-ligand interactions; conformational changes that accompany ligand release; secondary structure within the foot loop; and sequence variability within CLIC proteins. The table and figures have explanatory legends and they are discussed throughout the paper.

  1. Supplementary Materials