1H NMR spectroscopy reveals that mouse Hsp25 has a flexible C‐terminal extension of 18 amino acids

FEBS Letters

Gaestel, Matthias³  Carver, John A.¹  Schwedersky, Gabriele³  Esposito, Gennaro² 

[1] Australian Cataract Research Foundation, Department of Chemistry, The University of Wollongong, Wollongong, NSW, Australia;Dipartimento di Scienze e Tecnologie Biomediche, Università degli Studi di Udine, Udine, Italy;Max-Delbrück-Centrum für Molekulare Medizin, Berlin, Germany

关键词: Small heat-shock protein;    Chaperone;    α-Crystallin;    NMR spectroscopy;    Flexibility;   

DOI  :  10.1016/0014-5793(95)00770-A

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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, α-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 α-crystallin implying that both proteins have similar structures and that the C-terminal extensions could be of functional importance for both proteins.

【 授权许可】

Unknown