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 …

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 …

The overall charge content and the patterning of charged residues have a profound impact
on the conformational ensembles adopted by intrinsically disordered proteins. These …

A complete description of the pathways and mechanisms of protein folding requires a
detailed structural and energetic characterization of the conformational ensemble along the …

Biopharmaceutical formulations may be compromised by freezing, which has been
attributed to protein conformational changes at a low temperature, and adsorption to ice …

Allostery enables tight regulation of protein function in the cellular environment. Although
existing models of allostery are firmly rooted in the current structure–function paradigm, the …

The chemical shifts of backbone amide protons in proteins are sensitive reporters of local
structural stability and conformational heterogeneity, which can be determined from their …

Understanding protein folding mechanisms and their sequence dependence requires the
determination of residue-specific apparent kinetic rate constants for the folding and …

The presence and extent of hydrogen-bonding (H-bonding) cooperativity in proteins remains
a fundamental question, which in the past has been studied extensively, mostly by infrared …

Allostery is the phenomenon of coupling between distal binding sites in a protein. Such
coupling is at the crux of protein function and regulation in a myriad of scenarios, yet …