Fluorescence is the most widely used technique to study the effect of pressure on
biochemical systems. The use of pressure as a physical variable sheds light into volumetric …

Proteins are essential players in the vast majority of molecular level life processes. Since
their structure is in most cases substantial for their correct function, study of their structural …

High-pressure Fourier-transform infrared (FTIR) spectroscopy was used to determine the
pressure and temperature stability of Mal d1. This study was triggered by contradictory …

Volume changes that accompany protein unfolding and ligand binding are important but
largely neglected thermodynamic parameters that may facilitate rational drug design. Here …

Phosphoglycerate kinase (PGK) is a highly conserved enzyme that is crucial for glycolysis.
PGK is a monomeric protein composed of two similar domains and has been the focus of …

Hydrostatic pressure is a common perturbation to probe the conformations of proteins. There
are two common forms of pressure-dependent potentials of mean force (PMFs) derived from …

Along with temperature, pressure is the most important physical parameter determining the
thermodynamic properties and reactivity of chemical systems. In this work, we discuss the …

The mechanism by which conformational changes, particularly folding and unfolding, occur
in proteins and other biopolymers has been widely discussed in the literature. Molecular …

Partial molar volumes of amino acids in their zwitterionic and molecular forms were
calculated using molecular dynamics simulations of these systems in aqueous solutions …

Proteins must fold and function in the immensely complex environment of a cell, ie the
cytoplasm—this is far from the ideal test-tube setting of a dilute solution. Here, this thesis …