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

To be able to perform their biological function, a protein needs to be correctly folded into its
three dimensional structure. The protein folding process is spontaneous and does not …

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 …

Prion diseases, also known as transmissible spongiform encephalopathies, make up a
group of fatal neurodegenerative disorders linked with the misfolding and aggregation of the …

In domain-swapping, two or more identical protein monomers exchange structural elements
and fold into dimers or multimers whose units are structurally similar to the original …

The folding of many globular proteins from the unfolded (U) to the native (N) state appears to
be describable by a two-state N↔ U model, which has led to the general belief that protein …

Distinguishing between competing pathways of folding of a protein, on the basis of how they
differ in their progress of structure acquisition, remains an important challenge in protein …

Relating the amino acid composition and sequence to chain folding and binding
preferences of intrinsically disordered proteins (IDPs) has emerged as a huge challenge …

Understanding the origin of the cooperativity seemingly inherent in a folding or unfolding
reaction has been a major challenge. In particular, the relationship between folding …

Proteins, which behave as random coils in high denaturant concentrations undergo collapse
transition similar to polymers on denaturant dilution. We study collapse in the denatured …