Microsecond Backbone Motions Modulate the Oligomerization of the DNAJB6 Chaperone

DNAJB6 is a prime example of an anti-aggregation chaperone that functions as oligomer. oligomers are dynamic and subunit exchange critical for inhibiting client protein aggregation. The T193A mutation in the C-terminal domain (CTD) reduces both self-oligomerization proteins, has recently been linked to Parkinson's disease. Here, we show by NMR, including relaxation-based methods, minimal effects on structure β-stranded CTD but increases population rate formation partially folded state. results can be rationalized terms β-strand peptide plane flips occur timescale ≈100 μs lead global changes overall pleat/flatness CTD, thereby altering its ability oligomerize. These findings help forge link between dynamics, oligomerization activity which may possibly new therapeutic avenues tuned target specific substrates.