Fluorescence arguably constitutes the most widely used experimental approach in the field
of protein folding. Hence, any review of the use of fluorescence to probe protein stability and …

What are the molecular properties of proteins that fall on the radar of protein quality control
(PQC)? Here we mutate the E. coli's gene encoding dihydrofolate reductase (DHFR) and …

Here we investigated the effects of 2, 2, 2-trifluoroethanol (TFE) on the structure of α-
chymotrypsin. The protein aggregates maximally in 35%(v/v) TFE. Congo red and thioflavin …

Equilibrium guanidinium chloride-induced unfolding of bovine carbonic anhydrase NB has
been investigated by a combination of optical methods with size-exclusion chromatography …

Enzymes and motor proteins are dynamic macromolecules that coexist in a number of
conformations of similar energies. Protein function is usually accompanied by a change in …

We describe LINUS, a hierarchic procedure to predict the fold of a protein from its amino
acid sequence alone. The algorithm, which has been implemented in a computer program …

The overall structure of the transition-state and intermediate ensembles observed
experimentally for dihydrofolate reductase and interleukin-1β can be obtained by using …

Abstract Interaction with 8‐anilino‐1‐naphthalenesulfonate (ANS) is widely used to detect
molten globule states of proteins. We have found that even with stable partially folded states …

The kinetics of folding of a tryptophan containing mutant of the IgG binding domain of protein
L were characterized using stopped-flow circular dichroism, stopped-flow fluorescence, and …

The recent emphasis on rough energy landscapes for protein folding reactions by
theoreticians, and the many observations of complex folding kinetics by experimentalists …