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Cutting Off Functional Loops from Homodimeric Enzyme Superoxide Dismutase 1 (SOD1) Leaves Monomeric β-Barrels

Demetallation of the homodimeric enzyme Cu/Zn-superoxide dismutase (SOD1) is known to unleash pronounced dynamic motions in the long active-site loops that comprise almost a third of the folded structure. The resulting apo species, which shows increased propensity to aggregate, stands out as the pri...

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Bibliografische gegevens
Hoofdauteurs: Danielsson, Jens, Kurnik, Martin, Lang, Lisa, Oliveberg, Mikael
Formaat: Artigo
Taal:Inglês
Gepubliceerd in: American Society for Biochemistry and Molecular Biology 2011
Onderwerpen:
Online toegang:https://ncbi.nlm.nih.gov/pmc/articles/PMC3190884/
https://ncbi.nlm.nih.gov/pubmed/21700707
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M111.251223
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