The effect of the intersubunit disulfide bond on the structural and functional properties of the small heat shock protein Hsp25

The murine small heat shock protein Hsp25 carries a single cysteine residue in position 141 of its amino acid sequence. Interestingly, Hsp25 can exist within the cell as covalently bound dimer which is linked by an intermolecular disulfide bond between two monomers. Oxidative stress caused by treatm...

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Veröffentlicht in:	International journal of biological macromolecules 1998-05, Vol.22 (3), p.163-173
Hauptverfasser:	Zavialov, Anton, Benndorf, Rainer, Ehrnsperger, Monika, Zav’yalov, Vladimir, Dudich, Igor, Buchner, Johannes, Gaestel, Matthias
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals Chaperone Circular Dichroism Dimerization Dimerzation Disulfides - chemistry Drug Stability Heat-Shock Proteins - chemistry Heat-Shock Proteins - genetics Heat-Shock Proteins - physiology HSP27 Heat-Shock Proteins Humans In Vitro Techniques Mice Molecular Chaperones - chemistry Molecular Chaperones - genetics Molecular Chaperones - physiology Molecular Sequence Data Neoplasm Proteins - chemistry Neoplasm Proteins - genetics Neoplasm Proteins - physiology Oligomerization Oxidation-Reduction Oxidative Stress Protein Conformation Protein Structure, Secondary Recombinant Proteins - chemistry Recombinant Proteins - genetics Sequence Homology, Amino Acid Tumor Cells, Cultured
Online-Zugang:	Volltext
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