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 …

It is well-established that dynamics are central to protein function; their importance is
implicitly acknowledged in the principles of the Monod, Wyman and Changeux model of …

Protein dynamics take place on many time and length scales. Coarse‐grained structure‐
based \bf(G\overlineo) models utilize the funneled energy landscape theory of protein …

Most proteins consist of multiple domains. How do linkers efficiently transfer information
between sites that are on different domains to activate the protein? Mere flexibility only …

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 …

The frustratometer is an energy landscape theory-inspired algorithm that aims at quantifying
the location of frustration manifested in protein molecules. Frustration is a useful concept for …

Proteins can exist in a large number of conformations around their native states that can be
characterized by an energy landscape. The landscape illustrates individual valleys, which …

Proteins have often evolved sequences so as to acquire the ability for regulation via
allosteric conformational change. Here we investigate how allosteric dynamics is designed …

Energy landscape theories have provided a common ground for understanding the protein
folding problem, which once seemed to be overwhelmingly complicated. At the same time …