Folding kinetic pathway of phosphofructokinase-2 from Escherichia coli: A homodimeric enzyme with a complex domain organization

Article ID	Journal	Published Year	Pages	File Type
10871496	FEBS Letters	2011	7 Pages	PDF

Abstract

âº Folding mechanism of a large two-domain dimeric enzyme. âº A minimum kinetic model involves an unstructured monomer and dimeric intermediates. âº Most part of ÎASA occurs during a slow subunit association/folding step. âº Topological constrain between subunits and interface explains this behavior.

Keywords

ASA DTT dithiotreitol GdnHCl Subunit association Pfk-2 Subunit interface accessible surface area Folding kinetics Phosphofructokinase phosphofructokinase-2 Folding pathway Guanidine hydrochloride