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 …

To function, biomolecules require sufficient specificity of interaction as well as stability to live
in the cell while still being able to move. Thermodynamic stability of only a limited number of …

Natural protein domains must be sufficiently stable to fold but often need to be locally
unstable to function. Overall, strong energetic conflicts are minimized in native states …

▪ Abstract The energy landscape theory of protein folding is a statistical description of a
protein's potential surface. It assumes that folding occurs through organizing an ensemble of …

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 …

It has been recognized in the last few years that unstructured proteins play an important role
in biological organisms, often participating in signal transduction, transcriptional regulation …

Knowledge of the physical driving forces in proteins is essential for understanding their
structures and functions. As polymers, proteins have remarkable thermodynamic and kinetic …

The unfolded state and flexible linkers in the folded structure play essential roles in protein
stability and folding and protein− protein interactions. Intrinsic to these roles is the fact that …

Theory and simulations predict that the structural concert of protein folding reactions is
relatively low. Experimentally, folding cooperativity has been difficult to study, but in recent …

Protein molecules generally fold into precise threedimensional shapes. While of direct
interest to biochemists, the question of how folding occurs has attracted the interest of a …