Carver J A, Esposito G, Schwedersky G, Gaestel M
Australian Cataract Research Foundation, Department of Chemistry, University of Wollongong, NSW, Australia.
FEBS Lett. 1995 Aug 7;369(2-3):305-10. doi: 10.1016/0014-5793(95)00770-a.
The small heat-shock proteins (Hsps) exist as large aggregates and function by interacting and stabilising non-native proteins in a chaperone-like manner. Two-dimensional 1H NMR spectroscopy of mouse Hsp25 reveals that the last 18 amino acids have great flexibility with motion that is essentially independent of the domain core of the protein. The lens protein, alpha-crystallin, is homologous to Hsp25 and its two subunits also have flexible C-terminal extensions. The flexible region in Hsp25 encompasses exactly that expected from sequence comparison with alpha-crystallin implying that both proteins have similar structures and that the C-terminal extensions could be of functional importance for both proteins.
小分子热休克蛋白（Hsps）以大聚集体形式存在，并通过以伴侣样方式与非天然蛋白质相互作用并使其稳定来发挥功能。对小鼠Hsp25进行的二维¹H核磁共振光谱分析表明，其最后18个氨基酸具有很大的灵活性，其运动基本上独立于蛋白质的结构域核心。晶状体蛋白α-晶状体蛋白与Hsp25同源，其两个亚基也具有灵活的C端延伸。Hsp25中的柔性区域恰好与通过与α-晶状体蛋白进行序列比较所预期的区域一致，这意味着这两种蛋白质具有相似的结构，并且C端延伸对于这两种蛋白质可能具有功能重要性。
