Kinetics of the conformational cycle of Hsp70 reveals the importance of the dynamic and heterogeneous nature of Hsp70 for its function

Hsp70 is a conserved molecular chaperone that plays an indispensable role in regulating protein folding, translocation, and degradation. The conformational dynamics of Hsp70 and its regulation by cochaperones are vital to its function. Using bulk and singlemolecule fluorescence resonance energy tran...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 2020-04, Vol.117 (14), p.7814-7823
Hauptverfasser:	Wu, Si, 吴思, Hong, Liu, 洪柳, Wang, Yuqing, 王宇清, Yu, Jieqiong, 郁洁琼, Yang, Jie, 杨杰, 杨洁, Zhang, Hong, 张红, Perrett, Sarah, 柯莎
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine diphosphate Adenosine triphosphatase Adenosine triphosphate Binding Biological Sciences Dimerization Domains Energy transfer Fluorescence Fluorescence resonance energy transfer Heterogeneity Hsp40 protein Hsp70 protein Kinetics Nucleotides Protein folding Protein transport Psychological stress Stress concentration Substrates Translocation
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Schreiben Sie den ersten Kommentar!