Selective observation of semi-rigid non-core residues in dynamically complex mutant huntingtin protein fibrils

Selective observation of semi-rigid non-core residues in dynamically complex mutant huntingtin protein fibrils
J Struct Biol X. 2022 Nov 11;6:100077. doi: 10.1016/j.yjsbx.2022.100077. eCollection 2022.ABSTRACTMany amyloid-forming proteins, which are normally intrinsically disordered, undergo a disorder-to-order transition to form fibrils with a rigid β-sheet core flanked by disordered domains. Solid-state NMR (ssNMR) and cryogenic electron microscopy (cryoEM) excel at resolving the rigid structures within amyloid cores but studying the dynamically disordered domains remains challenging. This ... read more
Source: PubMedPublished on 2022-11-24By Irina Matlahov