Folding and stability of trp aporepressor from Escherichia coli

Equilibrium and kinetic studies of the urea-induced unfolding of trp aporepressor from Escherichia coli were performed to probe the folding mechanism of this intertwined, dimeric protein. The equilibrium unfolding transitions at pH 7.6 and 25 degrees C monitored by difference absorbance, fluorescenc...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	Biochemistry (Easton) 1990-07, Vol.29 (30), p.7011-7020
Hauptverfasser:	Gittelman, Mitchell S, Matthews, C. Robert
Format:	Artikel
Sprache:	eng
Schlagworte:	Apoproteins - chemistry Apoproteins - ultrastructure Bacterial Proteins Biological and medical sciences C.D Circular Dichroism Conformational dynamics in molecular biology Escherichia coli - analysis Escherichia coli Proteins Fundamental and applied biological sciences. Psychology Kinetics Models, Molecular Molecular biophysics Protein Conformation protein structure proteins Repressor Proteins - chemistry Repressor Proteins - ultrastructure Spectrometry, Fluorescence Spectrophotometry, Ultraviolet tertiary structure Thermodynamics
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Schreiben Sie den ersten Kommentar!