Small heat shock proteins (sHsps) are conserved across species and are important in stress
tolerance. Many sHsps exhibit chaperone-like activity in preventing aggregation of target …

The role of α-crystallin as a molecular chaperone may explain how the lens stays
transparent for so long. α-Crystallin prevents the aggregation of other lens crystallins and …

The small heat shock proteins (sHSPs) recently have been reported to have molecular
chaperone activity in vitro; however, the mechanism of this activity is poorly defined. We …

The majority of active tuberculosis cases arise as a result of reactivation of latent organisms
which are quiescent within the host. The ability of mycobacteria to survive extended periods …

Small Hsps (sHsps) encompass a widespread but diverse class of proteins. These low
molecular mass proteins (15—42 kDa) form dynamic oligomeric structures ranging from 9 to …

Small heat shock/α-crystallin proteins are defined by a conserved sequence of
approximately 90 amino acid residues, termed the α-crystallin domain, which is bounded by …

Publisher Summary The chapter presents a study on the chaperone-like properties of lens α-
crystalline. The most common source for lens α-crystallin has been cow or calf lens. The …

Background The two α-crystallins (αA-and αB-crystallin) are major components of our eye
lenses. Their key function there is to preserve lens transparency which is a challenging task …

The chaperone activity and biophysical properties of recombinant human αA-and αB-
crystallins were studied by light scattering and spectroscopic methods. While the chaperone …

Under conditions of stress, such as elevated temperature, molecular chaperones stabilize
proteins from unfolding, aggregating, and precipitating. We have investigated the chaperone …