FC0013
Heat-shock protein 25 (Hsp25)  -  α-lactalbumin

Biological function
Small heat shock proteins stabilize other proteins under stress conditions.

Structural evidence
The 18 residue long C-terminal tail of Hsp25 was proved to be disordered, even when interacting with α-lactalbumin. A slight peak broadening ¹H NMR TOCSY spectrum was observed, as an indicative of transient contacts with α- lactalbumin.

Biochemical evidence
Removal of the tail (Hsp25Δ18) diminished the ability of Hsp25 to stabilize its substrate.

Mechanism category
tethering

Significance
The fuzzy tail of Hsp25 is critical to chaperoning activity likely via solubilization of Hsp25.