Biophysical techniques used to characterise the oligomeric states of molecular chaperones and their interactions with amyloidogenic proteins.

Target	Technique	Experimental information	Ref.
Molecular chaperone oligomers	SEC	Size distribution	52, 82 and 83
	DLS	Hydrodynamic radius	79–81
	FCS	Hydrodynamic radius	86 and 87
	IM-MS	Population distribution and bimolecular structure in the gas phase	68, 71, 88 and 89
Chaperone–protein interactions	AUC	Molecular weight distribution	31, 32, 76–78
	sm-FRET	Interactions between biomolecules in close proximity (1–10 nm)	37, 38, 84 and 85
	NMR	Solution-state: structure, interactions, and dynamics of biomolecules Solid-state: structure of insoluble biomolecules	32 and 92–95
Fibril structure and chaperone binding	SAXS & SANS	Low-resolution protein structure in solution	96
	Immuno-EM	Structure and location of proteins in cells	31, 32, 90
	Cryo-EM	Structure of biomolecules, including amyloid fibrils and oligomeric proteins	67 and 91
Chaperone–fibril interactions	QCM	Molecular binding	50 and 83