Ja. Carver et al., H-1-NMR SPECTROSCOPY REVEALS THAT MOUSE HSP25 HAS A FLEXIBLE C-TERMINAL EXTENSION OF 18 AMINO-ACIDS, FEBS letters, 369(2-3), 1995, pp. 305-310
The small heat-shock proteins (Hsps) exist as large and stabilising no
n-native proteins in a chaperone-like manner. Two-dimensional H-1 NMR
spectroscopy of mouse Hsp25 reveals that the last 18 amino acids have
great flexibility with motion that is essentially independent of the d
omain care of the protein. The lens protein, alpha-crystallin, is homo
logous to Hsp25 and its two subunits also have flexible C-terminal ext
ensions. The flexible region in Hsp25 encompasses exactly that expecte
d from sequence comparison with alpha-crystallin implying that both pr
oteins have similar structures and that the C-terminal extensions coul
d be of functional importance for both proteins.