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Backbone NMR assignments of HypF-N under conditions generating toxic and non-toxic oligomers.

ABSTRACT: The HypF protein is involved in the maturation and regulation of hydrogenases. The N-terminal domain of HypF (HypF-N) has served as a key model system to study the pathways of protein amyloid formation and the nature of the toxicity of pre-fibrilar protein oligomers. This domain can aggregate into two forms of oligomers having significantly different toxic effects when added to neuronal cultures. Here, NMR assignments of HypF-N backbone resonances are presented in its native state and under the conditions favouring the formation of toxic and non-toxic oligomers. The analyses of chemical shifts provide insights into the protein conformational state and the possible pathways leading to the formation of different types of oligomers.

SUBMITTER: Patel JR

PROVIDER: S-EPMC6132818 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature

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Backbone NMR assignments of HypF-N under conditions generating toxic and non-toxic oligomers.

Patel Jayneil R JR Xu Yingqi Y Capitini Claudia C Chiti Fabrizio F De Simone Alfonso A

Biomolecular NMR assignments 20180521 2

The HypF protein is involved in the maturation and regulation of hydrogenases. The N-terminal domain of HypF (HypF-N) has served as a key model system to study the pathways of protein amyloid formation and the nature of the toxicity of pre-fibrilar protein oligomers. This domain can aggregate into two forms of oligomers having significantly different toxic effects when added to neuronal cultures. Here, NMR assignments of HypF-N backbone resonances are presented in its native state and under the ...[more]

PMID: 29786756

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