Charged and polar groups, through forming ion pairs, hydrogen bonds, and other less
specific electrostatic interactions, impart important properties to proteins. Modulation of the …

Salt bridges in proteins are bonds between oppositely charged residues that are sufficiently
close to each other to experience electrostatic attraction. They contribute to protein structure …

A very fast empirical method is presented for structure‐based protein pKa prediction and
rationalization. The desolvation effects and intra‐protein interactions, which cause variations …

Engineering proteins to withstand a broad range of conditions continues to be a coveted
objective, holding the potential to advance biomedicine, industry, and our understanding of …

Protein stability and function relies on residues being in their appropriate ionization states at
physiological pH. In situ residue pK as also provides a sensitive measure of the local protein …

The net charge and isoelectric pH (pI) of a protein depend on the content of ionizable groups
and their pK values. Ribonuclease Sa (RNase Sa) is an acidic protein with a pI= 3.5 that …

Thermal stability of proteins is crucial for both biotechnological and therapeutic applications.
Rational protein engineering therefore frequently aims at increasing thermal stability by …

Multiconformation continuum electrostatics (MCCE) explores different conformational
degrees of freedom in Monte Carlo calculations of protein residue and ligand pKas. Explicit …

How proteins sense and navigate the cellular interior to find their functional partners remains
poorly understood. An intriguing aspect of this search is that it relies on diffusive encounters …

Salt bridges have been proposed to play a crucial role in promoting hyperthermostability in
proteins, yet they appear to make little contribution to protein stability at room temperature …