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The coupling between disulphide status, metallation and dimer interface strength in Cu/Zn superoxide dismutase.
Umeå University, Faculty of Medicine, Medical Biosciences, Clinical chemistry.
2007 (English)In: J Mol Biol, ISSN 0022-2836, Vol. 365, no 2, 333-42 p.Article in journal (Refereed) Published
Place, publisher, year, edition, pages
2007. Vol. 365, no 2, 333-42 p.
Keyword [en]
Copper/*chemistry, Crystallography; X-Ray, Cytotoxins/*chemistry, Disulfides/*chemistry, Enzyme Stability, Humans, Models; Structural, Mutation, Protein Folding, Protein Structure; Quaternary, Protein Structure; Tertiary, Structure-Activity Relationship, Superoxide Dismutase/*chemistry/genetics, X-Ray Diffraction, Zinc/*chemistry
URN: urn:nbn:se:umu:diva-7584PubMedID: 17070542OAI: diva2:147255
Available from: 2008-01-11 Created: 2008-01-11 Last updated: 2011-01-11Bibliographically approved

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