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Updated: Mar 6, 2026

Combining Wet and Dry Lab Techniques to Guide the Crystallization of Large Coiled-coil Containing Proteins
Published on: January 6, 2017
α-Crystallins Are Small Heat Shock Proteins: Functional and Structural Properties
T S Tikhomirova1, O M Selivanova, O V Galzitskaya
1Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, 142290, Russia. ogalzit@vega.protres.ru.
Abstract:
During its life cycle, a cell can be subjected to various external negative effects. Many proteins provide cell protection, including small heat shock proteins (sHsp) that have chaperone-like activity. These proteins have several important functions involving prevention of apoptosis and retention of cytoskeletal integrity; also, sHsp take part in the recovery of enzyme activity. The action mechanism of sHsp is based on the binding of hydrophobic regions exposed to the surface of a molten globule. α-Crystallins presented in chordate cells as two αA- and αB-isoforms are the most studied small heat shock proteins. In this review, we describe the main functions of α-crystallins, features of their secondary and tertiary structures, and examples of their partners in protein-protein interactions.
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