This title appears in the Scientific Report : 2011 

Native and unfolded states of phosphoglycerate kinase studied by single molecule FRET
Rosenkranz, T.
Schlesinger, R. / Gabba, M. / Fitter, J.
Molekulare Biophysik; ICS-5
ChemPhysChem, 12 (2011) S. 704 - 710
Weinheim Wiley-VCH Verl. 2011
704 - 710
10.1002/cphc.201000701
21344599
Journal Article
BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung
ChemPhysChem 12
J
Please use the identifier: http://dx.doi.org/10.1002/cphc.201000701 in citations.
Single-molecule Förster resonance energy transfer (FRET) measurements with phosphoglycerate kinase from yeast were performed at different concentrations of guanidine hydrochloride. From these steady-state measurements we obtained FRET efficiency histograms characterizing structural properties of individual proteins at different stages between the native and the fully unfolded state. Native proteins exhibit a slightly more expanded structure under buffer conditions without denaturant as compared to conditions with denaturant. At 0.5 M GndHCl an unfolded state population that exhibits a significantly expanded structure as compared to the native state, emerges. The unfolded state is characterized by a pronounced broadening of the efficiency distribution, which indicates a large structural and/or dynamical heterogeneity within the population. At high denaturant concentrations, well above the unfolding transition at C(1/2)~0.7 M, we observe a progressive expansion of the protein structure, namely globule-coil transition.