Specificity in chaperonin-mediated protein folding

Chaperonins are ubiquitous multisubunit toroidal complexes that aid protein folding in an ATP-dependent manner. Current models of folding by the bacterial chaperonin GroEL depict its role as unfolding and releasing molecules that have misfolded, so that they can return to a potentially productive fo...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	Nature (London) 1995-05, Vol.375 (6528), p.250-253
Hauptverfasser:	Tian, Guoling, Vainberg, Irina E, Tap, William D, Lewis, Sally A, Cowan, Nicholas J
Format:	Artikel
Sprache:	eng
Schlagworte:	Actins - metabolism Adenosine Triphosphate - metabolism ATP Bacteria Biochemistry Biological and medical sciences Chaperonin 10 - metabolism Chaperonin 60 - metabolism Chaperonins - metabolism Conformational dynamics in molecular biology Cytosol - metabolism Endopeptidase K Escherichia coli Escherichia coli - metabolism Fundamental and applied biological sciences. Psychology Molecular biophysics Molecules Protein Binding Protein Folding Proteins Serine Endopeptidases - metabolism Tubulin - metabolism
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Schreiben Sie den ersten Kommentar!