Disrupted protein folding or decreased protein stability can lead to the accumulation of
(partially) un‐or misfolded proteins, which ultimately cause the formation of protein …

Circular dichroism (CD) is being increasingly recognised as a valuable technique for
examining the structure of proteins in solution. However, the value of many studies using CD …

Denaturant m values, the dependence of the free energy of unfolding on denaturant
concentration, have been collected for a large set of proteins. The m value correlates very …

In this review, we shall outline the basic principles Ž. of circular dichroism CD and indicate
the types of structural information relevant to the study of the Ž. folding and unfolding or …

The effects of urea on protein stability have been studied using a model system in which we
have determined the energetics of dissolution of a homologous series of cyclic dipeptides …

We use a combination of experiments, computer simulations and simple model calculations
to characterize, first, the folding transition state ensemble of the src SH3 domain, and …

The protein engineering analysis of the α-spectrin SH3 domain at three different stability
conditions (pH 7.0, 3.5 and 2.5) reveals a folding transition state structured around the distal …

Relaxation rates for folding and unfolding of two proteins have been measured over a range
of denaturant concentrations to examine the reaction pathways leading to the late transition …

The urea, guanidine hydrochloride, salt, and temperature dependence of the rate of
dissociation of CO from a nonequilibrium state of CO-bound native ferrocytochrome c has …

We have analyzed the existence of obligatory steps in the folding reaction of the α-spectrin
SH3 domain by mutating Asp 48 (D48G), which is at position i+ 3 of an isolated two-residue …