Proteins have dynamic structures that undergo chain motions on time scales spanning from
picoseconds to seconds. Resolving the resultant conformational heterogeneity is essential …

A thermodynamically and kinetically simple picture of protein folding envisages only two
states, native (N) and unfolded (U), separated by a single activation free energy barrier, and …

Ankyrin repeat proteins are found in all three kingdoms of life. Fundamentally, these proteins
are involved in protein-protein interaction in order to activate or suppress biological …

Protein folding and unfolding experiments are interpreted under the assumption of
microscopic reversibility, that is, that at equilibrium one process is the reverse of the other …

Despite the recent advances in the prediction of protein structures by deep neutral networks,
the elucidation of protein-folding mechanisms remains challenging. A promising theory for …

Statistical mechanical models that afford an intermediate resolution between macroscopic
chemical models and all-atom simulations have been successful in capturing folding …

The term allostery was originally developed to describe structural changes in one binding
site induced by the interaction of a partner molecule with a distant binding site, and it has …

Protein sequences and structures evolve by satisfying varied physical and biochemical
constraints. This multi-level selection is enabled not just by the patterning of amino acids on …

Experimental determination of the key features of the free energy landscapes of proteins,
which dictate their adeptness to fold correctly, or propensity to misfold and aggregate and …

How many structurally different microscopic routes are accessible to a protein molecule
while folding? This has been a challenging question to address experimentally as single …