We have studied two misfolded oligomeric forms of the protein HypF-N, which show similar morphologies but very different toxicities. We measured over 80 intermolecular distance-dependent parameters for each oligomer type using FRET, in conjunction with solution- and solid-state NMR and other biophysical techniques. The results indicate that the formation of a highly organised hydrogen bonded core in the toxic oligomers results in the exposure of a larger number of hydrophobic residues than in the nontoxic species, causing the former to form aberrant interactions with cellular components.
Capitini, C., Patel, J., Natalello, A., D'Andrea, C., Relini, A., Jarvis, J., et al. (2018). Structural differences between toxic and nontoxic HypF-N oligomers. CHEMICAL COMMUNICATIONS, 54(62), 8637-8640 [10.1039/c8cc03446j].
Structural differences between toxic and nontoxic HypF-N oligomers
Natalello A.Membro del Collaboration Group
;
2018
Abstract
We have studied two misfolded oligomeric forms of the protein HypF-N, which show similar morphologies but very different toxicities. We measured over 80 intermolecular distance-dependent parameters for each oligomer type using FRET, in conjunction with solution- and solid-state NMR and other biophysical techniques. The results indicate that the formation of a highly organised hydrogen bonded core in the toxic oligomers results in the exposure of a larger number of hydrophobic residues than in the nontoxic species, causing the former to form aberrant interactions with cellular components.
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