Experimental studies have demonstrated that many small, single-domain proteins fold via
simple two-state kinetics. We present a first principles approach for predicting these …

Circular dichroism (CD) is a useful spectroscopic technique for studying the secondary
structure, folding and binding properties of proteins. This protocol covers how to use the …

Fig. 1 Correlation between the observed values of log kf and the crossvalidated predictions.
Blue symbols are for models that take the contact order as their only input (triangles for α …

Human serum albumin (HSA) contains three α-helical domains (I–III). The unfolding process
of these domains was monitored using covalently bound fluorescence probes; domain I was …

Folding and unfolding rates have been measured for the peripheral subunit-binding domain,
a small three-helix protein. The protein folds very fast, with rates too rapid to be measured …

Cold denaturation is a general property of globular proteins, but it is difficult to directly
characterize because the transition temperature of protein cold denaturation, T c, is often …

pH-dependent studies of the folding kinetics and stability of a set of His to Gln point mutants
were used to characterize the denatured state and transition state ensembles for the C …

The folding kinetics and thermodynamics of the isolated C-terminal domain of the ribosomal
protein L9 (CTL9) have been studied as a function of pH. CTL9 is an α–β protein that …

Cold unfolding of proteins is predicted by the Gibbs–Helmholtz equation and is thought to be
driven by a strongly temperature-dependent interaction of protein nonpolar groups with …

The stability of the isolated C-terminal domain of the ribosomal protein L9 (CTL9) is strongly
dependent upon pH. Below pH 4.2, the folded and unfolded states are both populated …