Protein misfolding and aggregation is observed in many amyloidogenic diseases affecting
either the central nervous system or a variety of peripheral tissues. Structural and dynamic …

An antibody's stability greatly influences its performance (ie its specificity and affinity). Thus,
stability is a major issue for researchers and manufacturers, especially with the increasing …

The receptor-binding domain (RBD) of the SARS-CoV-2 spike protein plays a crucial role in
binding the human cell receptor ACE2 that is required for viral entry. Many studies have …

The aversion of hydrophobic solutes for water drives diverse interactions and assemblies
across materials science, biology, and beyond. Here, we review the theoretical …

We study the properties of water at the surface of an antifreeze protein with femtosecond
surface sum frequency generation spectroscopy. We find clear evidence for the presence of …

The conformation of water around proteins is of paramount importance, as it determines
protein interactions. Although the average water properties around the surface of proteins …

The understanding of the complex conformational landscape of amyloid aggregation and its
modulation by relevant physicochemical and cellular factors is a prerequisite for elucidating …

Hydration water on the surface of a protein is thought to mediate the thermodynamics of
protein–ligand interactions. For hydration water to play a role beyond modulating global …

Folding funnel is the essential concept of the free energy landscape for ordered proteins.
How does this concept apply to intrinsically disordered proteins (IDPs)? Here, we address …

Recent advances in machine learning technologies and their applications have led to the
development of diverse structure–property relationship models for crucial chemical …