Intrinsically disordered protein regions (IDRs)-regions that do not fold into a fixed three-
dimensional structure but instead exist in a heterogeneous ensemble of conformations-have …

A variety of excipients are used to stabilize proteins, suppress protein aggregation, reduce
surface adsorption, or to simply provide physiological osmolality. The stabilizers encompass …

Osmolytes are small organic compounds that affect protein stability and are ubiquitous in
living systems. In the equilibrium protein folding reaction, unfolded (U)⇌ native (N) …

The study of the interactions of salts and osmolytes with macromolecules in aqueous
solution originated with experiments concerning protein precipitation more than 100 years …

Under physiological conditions, a protein undergoes a spontaneous disorder⇌ order
transition called “folding.” The protein polymer is highly flexible when unfolded but adopts its …

A primary thermodynamic goal in protein biochemistry is to attain predictive understanding
of the detailed energetic changes that are responsible for folding/unfolding. Through use of …

We seek to understand the link between protein thermodynamics and protein structure in
molecular detail. A classical approach to this problem involves assessing changes in protein …

The mechanism by which urea and guanidinium destabilize protein structure is
controversial. We tested the possibility that these denaturants form hydrogen bonds with …

Protein stability often is studied in vitro through the use of urea and guanidinium chloride,
chemical cosolvents that disrupt protein native structure. Much controversy still surrounds …

In adaptation biology the discovery of intracellular osmolyte molecules that in some cases
reach molar levels, raises questions of how they influence protein thermodynamics. We've …