Temperature dependence of chaperone-like activity and oligomeric state of αB-crystallin

Effect of disulfide crosslinking on thermal transitions and chaperone-like activity of human small heat shock protein HspB1

“…Deletion of the first 14 or 24 residues completely prevented temperaturedependent self-association of HspB1 (Lelj-Garolla and Mauk 2012), and therefore, it was supposed that the Nterminal extension plays an important role in HspB1 selfassociation. Similar temperature-dependent self-association was also reported for αB-crystallin (Spinozzi et al 2006;Skouri-Panet et al 2006;Aquilina et al 2013).…”

Structural perturbation of αB-crystallin by zinc and temperature related to its chaperone-like activity

“…In other words, ␣B-crystallin passes from a "compact" state at 25 • C to a "swollen" state at 37 • C. This structural transition can be hypothesized to account for the increasing chaperone-like activity when the protein is brought from 25 to 37 • C, as already observed [52].…”

Structural Properties of Silkworm Small Heat-Shock Proteins: sHSP19.9 and sHSP20.8

“…The increase in the size of sHSP19.9 in the presence of DTT was fitted to a curve with the transition temperature at 41-42 C. The transition temperature of the increase in the size of sHSP20.8 was about 40 C regardless of the presence of DTT. It has been reported that the Rg value of human B-crystallin increases at temperatures above 42 C. 35) Human Hsp27 perhaps also shows a temperaturedependent increase in size, based on increases in the value of the sedimentation coefficient. 36) The molecular sizes of sHSP19.9 and sHSP20.8 increased with increasing temperature like B-crystallin and Hsp27.…”