Interaction of hsp70 with Unfolded Proteins: Effects of Temperature and Nucleotides on the Kinetics of Binding

Circular dichroism and HPLC gel filtration were used to show that cytosolic hsp70 is thermally stable but undergoes a conformational transition (midpoint, 43⚬C; 57⚬C in the presence of ATP or ADP) leading to oligomerization. hsp70 binds to unfolded, but not to folded, proteins in a temperature-depen...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 1991-07, Vol.88 (13), p.5719-5723
Hauptverfasser:	Palleros, Daniel R., Welch, William J., Fink, Anthony L.
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Diphosphate - metabolism Adenosine Triphosphatases - metabolism Adenosine Triphosphate - metabolism Animals Biochemistry Biological and medical sciences Cattle Circular Dichroism Dimers Fundamental and applied biological sciences. Psychology Heat-Shock Proteins - metabolism HeLa cells Hot Temperature Humans In Vitro Techniques Interactions. Associations Intermolecular phenomena Kinetics Lactalbumin - metabolism Micrococcal Nuclease - metabolism Molecular biophysics Nucleotides Oligomers Protein Binding Protein Conformation Protein Denaturation Staphylococcus Thermal stability Trimers
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