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

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

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

Biomol NMR Assign. 2018 May 21;:

Authors: Patel JR, Xu Y, Capitini C, Chiti F, De Simone A

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.


PMID: 29786756 [PubMed - as supplied by publisher]



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