Water is an essential participant in the stability, structure, dynamics, and function of proteins
and other biomolecules. Thermodynamically, changes in the aqueous environment affect …

In his memorable book published in 1949, The Physics of High Pressure, 1 Bridgman states
that “it is a well-known result of thermodynamics that a substance is only completely …

Although it is now relatively well understood how sequence defines and impacts global
protein stability in specific structural contexts, the question of how sequence modulates the …

Time-resolved experiments demand high resolution both in spectral dimensions and in time
of the studied kinetic process. The latter requirement traditionally prohibits applications of …

In unfolded proteins, peptide bonds involving Pro residues exist in equilibrium between the
minor cis and major trans conformations. Folded proteins predominantly contain trans‐Pro …

In general, small proteins rapidly fold on the timescale of milliseconds or less. For proteins
with a substantial volume difference between the folded and unfolded states, their …

High pressure (HP) or urea is commonly used to disturb folding species. Pressure favors the
reversible unfolding of proteins by causing changes in the volumetric properties of the …

Phosphoglycerate kinase has been a model for the stability, folding cooperativity and
catalysis of a two-domain protein. The human isoform 1 (hPGK1) is associated with cancer …

NMR spectroscopy is particularly adept at site-specifically monitoring dynamic processes in
proteins, such as protein folding, domain movements, ligand binding, and side-chain …

High-pressure is a well-known perturbation method used to destabilize globular proteins. It
is perfectly reversible, which is essential for a proper thermodynamic characterization of a …