Diffuse binding of Zn2+ to the denatured ensemble of Cu/Zn superoxide dismutase 1
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- 作者：Scarlett Szpryngiel ; Mikael Oliveberg ; Lena Mä ; ler ; lena.maler@dbb.su.se" class="auth_mail" title="E-mail the corresponding author
- 关键词：SOD1 ; superoxide dismutase 1 ; HSQC ; heteronuclear single-quantum coherence ; TOCSY ; total correlation spectroscopy ; NOESY ; nuclear Overhauser enhancement spectroscopy ; IDP ; intrinsically disordered protein
- 刊名：FEBS Open Bio
- 出版年：2015
- 出版时间：2015
- 年：2015
- 卷：5
- 期：Complete
- 页码：56-63
- 全文大小：1407 K
文摘
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Nearly complete backbone assignments for monomeric SOD1 were obtained.
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Monomeric SOD1 is unstructured in 9 M urea.
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Zn2+-binding to monomeric SOD1 occurs through diffuse coordination to most His residues.
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The binding geometry of Zn2+ is different than in the native, folded SOD1.