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

It has long been axiomatic that a protein's structure determines its function. Intrinsically
disordered proteins (IDPs) and disordered protein regions (IDRs) defy this structure …

Proteins are important food ingredients that possess both functional and nutritional
properties. High hydrostatic pressure (HHP) is an emerging nonthermal food processing …

Liquid–liquid phase separation (LLPS) of proteins and other biomolecules play a critical role
in the organization of extracellular materials and membrane‐less compartmentalization of …

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 …

Background Molecular dynamics (MD) simulation is well-recognized as a powerful tool to
investigate protein structure, function, and thermodynamics. MD simulation is also used to …

Hypothesis High hydrostatic pressure treatment causes structural changes in interfacial-
active β-lactoglobulin (β-lg). We hypothesized that the pressure-induced structural changes …

The binding capacity of β-Lactoglobulin (BLG) is crucial for delivering polyphenols,
influenced by structural changes. High pressure processing (HPP) has the potential to …

We investigated the combined effects of temperature and pressure on liquid–liquid phase
separation (LLPS) phenomena of α‐elastin up to the multi‐kbar regime. FT‐IR spectroscopy …

Hydrostatic pressure alters the free energy of proteins by a few kJ mol− 1, with the amount
depending on their partial molar volumes. Because the folded ground state of a protein …