The Conformational Dynamics of the Mitochondrial Hsp70 Chaperone

Heat shock proteins 70 (Hsp70) represent a ubiquitous and conserved family of molecular chaperones involved in a plethora of cellular processes. The dynamics of their ATP hydrolysis-driven and cochaperone-regulated conformational cycle are poorly understood. We used fluorescence spectroscopy to anal...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	Molecular cell 2010-04, Vol.38 (1), p.89-100
Hauptverfasser:	Mapa, Koyeli, Sikor, Martin, Kudryavtsev, Volodymyr, Waegemann, Karin, Kalinin, Stanislav, Seidel, Claus A.M., Neupert, Walter, Lamb, Don C., Mokranjac, Dejana
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Diphosphate - chemistry Adenosine Diphosphate - metabolism Adenosine Triphosphate - chemistry Adenosine Triphosphate - metabolism Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Calcium-Transporting ATPases - chemistry Calcium-Transporting ATPases - metabolism Escherichia coli Proteins - chemistry Escherichia coli Proteins - genetics Escherichia coli Proteins - metabolism Fluorescence Resonance Energy Transfer HSP40 Heat-Shock Proteins - chemistry HSP40 Heat-Shock Proteins - metabolism HSP70 Heat-Shock Proteins - chemistry HSP70 Heat-Shock Proteins - genetics HSP70 Heat-Shock Proteins - metabolism Humans Membrane Proteins - chemistry Membrane Proteins - metabolism Mitochondria - metabolism Models, Molecular Molecular Chaperones - chemistry Molecular Chaperones - metabolism Protein Conformation Protein Folding PROTEINS Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - metabolism
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Schreiben Sie den ersten Kommentar!