Artist impression of Hsp70 that clamps a folded substrate protein (green) between two domains (orange and yellow). The third (purple) is the ATP binding domain of Hsp70. Tans and his colleagues discovered that Hsp70 not only binds unfolded chain segments, which destabilizes folded proteins. It can also do the opposite: to bind and stabilize folded protein states. This finding has implications for the many physiological roles of Hsp70 in cells.
Image credits: M. Avellaneda & S. Tans

Artist impression of Hsp70 that clamps a folded substrate protein (green) between two domains (orange and yellow). The third (purple) is the ATP binding domain of Hsp70. Tans and his colleagues discovered that Hsp70 not only binds unfolded chain segments, which destabilizes folded proteins. It can also do the opposite: to bind and stabilize folded protein states. This finding has implications for the many physiological roles of Hsp70 in cells.
Image credits: M. Avellaneda & S. Tans