Structural differences between toxic and nontoxic HypF-N oligomers. Issue 62 (18th July 2018)

• Record Type: Journal Article
• Authors: 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
• Is Part Of: Chemical communications. Volume 54:Issue 62(2018)
• Page Start: 8637
• Page End: 8640
• Publication Date: 2018-07-18
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1039/c8cc03446j
• Languages: English
• ISSNs: 1359-7345

Abstract

Abstract : We have studied two misfolded oligomeric forms of the protein HypF-N, which show similar morphologies but very different toxicities. 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.