All soluble proteins populate conformational ensembles that together constitute the native
state. Their fluctuations in water are intrinsic thermodynamic phenomena, and the …

When Szent-Györgyi called water the “matrix of life”, 1 he was echoing an old sentiment.
Paracelsus in the 16th century said that “water was the matrix of the world and of all its …

Some frequently encountered deficiencies in all-atom molecular simulations, such as
nonspecific protein–protein interactions being too strong, and unfolded or disordered states …

Water is essential for life in many ways, and without it biomolecules might no longer truly be
biomolecules. In particular, water is important to the structure, stability, dynamics, and …

Biomolecular condensation is a key mechanism for organizing cellular processes in a
spatiotemporal manner. The phase-transition nature of this process defines a density …

Hydroxyl radical protein footprinting (HRPF) coupled to mass spectrometry has been
successfully used to investigate a plethora of protein-related questions. The method, which …

Proteins perform their biological functions through motion. Although high throughput
prediction of the three-dimensional static structures of proteins has proved feasible using …

Biomolecules are the prime information processing elements of living matter. Most of these
inanimate systems are polymers that compute their own structures and dynamics using as …

Energetic local frustration offers a biophysical perspective to interpret the effects of
sequence variability on protein families. Here we present a methodology to analyze local …

We propose a method of quantifying the degree of frustration manifested by spatially local
interactions in protein biomolecules. This method of localization smoothly generalizes the …