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.
Structural differences between toxic and nontoxic HypF-N oligomers / Capitini, Claudia; Patel, Jayneil R.; Natalello, Antonino; D'Andrea, Cristiano; Relini, Annalisa; Jarvis, James A.; Birolo, Leila; Peduzzo, Alessia; Vendruscolo, Michele; Matteini, Paolo; Dobson, Christopher M.; De Simone, Alfonso; Chiti, Fabrizio. - In: CHEMICAL COMMUNICATIONS. - ISSN 1359-7345. - 54:62(2018), pp. 8637-8640. [10.1039/c8cc03446j]
Structural differences between toxic and nontoxic HypF-N oligomers
Birolo, Leila;De Simone, Alfonso;
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.File | Dimensione | Formato | |
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