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 …

Polypeptide chain collapse is an integral component of a protein folding reaction. In this
review, experimental characterization of the interplay of polypeptide chain collapse …

Coincidental equilibrium unfolding transitions observed by multiple structural probes are
taken to justify the modeling of protein unfolding as a two-state, N⇌ U, cooperative process …

An unresolved question in the field of protein folding is whether a protein unfolds in a two-
state (N↔ U) cooperative manner with only two species being populated during the entire …

LEN is a κIV immunoglobulin light chain variable domain from a patient suffering from
multiple myeloma but with no evidence of amyloid fibrils. However, fibrils are formed when …

The fluorescence properties of three variants of α-lactalbumin (α-LA) containing a single
tryptophan residue were investigated under native, molten globule, and unfolded conditions …

The recent application of 19F NMR in the study of biomolecular structure and dynamics has
made it a potentially attractive probe to complement traditional 15N/13C labelled probes for …

Structural analysis of the initial steps in protein folding is difficult because of the swiftness
with which these steps occur. Hence, the link between initial polypeptide chain collapse and …

Dissecting a protein unfolding process into individual steps can provide valuable information
on the forces that maintain the integrity of the folded structure. Solvation of the protein core …

There is a need for an intrinsic spectral probe to monitor key events like protein unfolding
and aggregation in a rapid and unambiguous manner. Protein aggregation is an important …