SOD1 exhibits allosteric frustration to facilitate metal binding affinity

@article{Das2013SOD1EA,
  title={SOD1 exhibits allosteric frustration to facilitate metal binding affinity},
  author={Atanu Kumar Das and Steven S. Plotkin},
  journal={Proceedings of the National Academy of Sciences},
  year={2013},
  volume={110},
  pages={3871 - 3876}
}
  • A. Das, S. Plotkin
  • Published 6 January 2013
  • Biology
  • Proceedings of the National Academy of Sciences
Superoxide dismutase–1 (SOD1) is a ubiquitous, Cu and Zn binding, free-radical defense enzyme whose misfolding and aggregation play a potential key role in amyotrophic lateral sclerosis, an invariably fatal neurodegenerative disease. Over 150 mutations in SOD1 have been identified with a familial form of the disease, but it is presently not clear what unifying features, if any, these mutants share to make them pathogenic. Here, we develop several unique computational assays for probing the… 

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