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.
Backbone NMR assignments of HypF-N under conditions generating toxic and non-toxic oligomers / Patel, Jayneil R.; Xu, Yingqi; Capitini, Claudia; Chiti, Fabrizio; De Simone, Alfonso*. - In: BIOMOLECULAR NMR ASSIGNMENTS. - ISSN 1874-2718. - STAMPA. - 12:(2018), pp. 273-277. [10.1007/s12104-018-9822-7]
Backbone NMR assignments of HypF-N under conditions generating toxic and non-toxic oligomers
Capitini, Claudia;Chiti, Fabrizio;
2018
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.File | Dimensione | Formato | |
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