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 …

There are several proteins, which can cause allergic reaction if they are inhaled or ingested.
Our everyday food can also contain such proteins. Food allergy is an IgE-mediated immune …

It is well known that high hydrostatic pressures can induce the unfolding of proteins. The
physical underpinnings of this phenomenon have been investigated extensively but remain …

Ionizable residues can release and take up protons and this has an influence on protein
structure and function. The extent of protonation is linked to the overall pH of the solution …

Pressure and temperature are the two fundamental variables of thermodynamics.
Temperature and chemical perturbation are central experimental tools for the exploration of …

Although our knowledge of static and/or average folded structures of proteins has increased
dramatically in recent years thanks to the development of X-ray crystallography and solution …

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

Structural consequences of ionization of residues buried in the hydrophobic interior of
proteins were examined systematically in 25 proteins with internal Lys residues. Crystal …

The folding of staphylococcal nuclease (SNase) is known to proceed via a major
intermediate in which the central OB subdomain is folded and the C-terminal helical …

Fish allergy is associated with IgE-mediated hypersensitivity reactions to parvalbumins,
which are small calcium-binding muscle proteins and represent the major and sole …