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

John A. Carver, Gennaro Esposito, Gabriele Schwedersky, Matthias Gaestel

Research output: Contribution to journalArticle

Abstract

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.

Original languageEnglish (US)
Pages (from-to)305-310
Number of pages6
JournalFEBS Letters
Volume369
Issue number2-3
DOIs
StatePublished - Aug 7 1995

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Crystallins
Nuclear magnetic resonance spectroscopy
Magnetic Resonance Spectroscopy
Amino Acids
Small Heat-Shock Proteins
Proteins
Proton Magnetic Resonance Spectroscopy

Keywords

  • Chaperone
  • Flexibility
  • NMR spectroscopy
  • Small heat-shock protein
  • α-Crystallin

ASJC Scopus subject areas

  • Structural Biology
  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this

1H NMR spectroscopy reveals that mouse Hsp25 has a flexible C-terminal extension of 18 amino acids. / Carver, John A.; Esposito, Gennaro; Schwedersky, Gabriele; Gaestel, Matthias.

In: FEBS Letters, Vol. 369, No. 2-3, 07.08.1995, p. 305-310.

Research output: Contribution to journalArticle

Carver, John A. ; Esposito, Gennaro ; Schwedersky, Gabriele ; Gaestel, Matthias. / 1H NMR spectroscopy reveals that mouse Hsp25 has a flexible C-terminal extension of 18 amino acids. In: FEBS Letters. 1995 ; Vol. 369, No. 2-3. pp. 305-310.
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