Premium
1 H NMR spectroscopy reveals that mouse Hsp25 has a flexible C‐terminal extension of 18 amino acids
Author(s) -
Carver John A.,
Esposito Gennaro,
Schwedersky Gabriele,
Gaestel Matthias
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00770-a
Subject(s) - nuclear magnetic resonance spectroscopy , amino acid , heat shock protein , chaperone (clinical) , chemistry , protein superfamily , peptide sequence , biophysics , biochemistry , crystallography , biology , stereochemistry , medicine , pathology , gene
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 1 H 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.