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

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

Transient receptor potential vanilloid member 1 (TRPV1) is a Ca2+-permeable cation
channel that serves as the primary heat and capsaicin sensor in humans. Using cryo-EM, we …

Escherichia coli is one of the organisms of choice for the production of recombinant proteins.
Its use as a cell factory is well-established and it has become the most popular expression …

Our goal was to gain a better understanding of the contribution of the burial of polar groups
and their hydrogen bonds to the conformational stability of proteins. We measured the …

Forces to reckon with: Supramolecular complexes, such as the one shown, are normally
based on a combination of different interactions such as ion pairing, hydrogen bonds, and …

A complete inventory of the forces governing protein folding is critical for productive protein
modeling, including structure prediction and de novo design, as well as understanding …

Proteins are marginally stable, and the folding/unfolding equilibrium of proteins in aqueous
solution can easily be altered by the addition of small organic molecules known as …

More than three-quarters of the Earth's surface is occupied by cold ecosystems, including
the ocean depths, and polar and alpine regions. These permanently cold environments …

A Gaussian solvent‐exclusion model for the solvation free energy is developed. It is based
on theoretical considerations and parametrized with experimental data. When combined …