Per-Ola Freskgård

TL;DR: Prolyl isomerase, which has been shown to accelerate rate-limiting cis-trans peptidyl-proline isomerization steps in the folding pathway, can also participate in the protein-folding process as a chaperone.

TL;DR: The circular dichroism (CD) spectrum of human carbonic anhydrase II has been investigated using various mutants of the enzyme in which tryptophans have been replaced by site-directed mutagenesis, showing that the tryptophile are the major determinant for this part of the CD spectrum.

TL;DR: It is shown that human carbonic anhydrase II forms a stable and compact folding intermediate at a moderate concentration of guanidine hydrochloride, and results indicate that the folding intermediate has an ordered native-like secondary structure in the central part of the beta-sheet, whereas the peripheral parts of thebeta-sheet seems to be less ordered.

TL;DR: Measurements were made of fluorescence spectra produced by pseudo-wild-type human carbonic anhydrase II and mutants in which the tryptophan residues had been replaced by phenylalanine or cysteine residues and results indicate that the part of the native protein that corresponds to beta-strands 3-7 forms a compact core in a molten globule intermediate.

TL;DR: The result suggests that surface induced unfolding may give rise to intermediates similar to those for unfolding induced by, for example GuHCl, the intermediate observed has some features of the molten globule.