Backbone NMR assignments of HypF-N under conditions generating toxic and non-toxic oligomers.
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] More... |
All times are GMT. The time now is 02:05 PM. |
Powered by vBulletin® Version 3.7.3
Copyright ©2000 - 2024, Jelsoft Enterprises Ltd.
Search Engine Friendly URLs by vBSEO 3.6.0
Copyright, BioNMR.com, 2003-2013