English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

The letter by Candel et al. (1) does not address a potential problem with their own experimental set-up. In particular, the use of guanidinium hydrochloride (GdnHCl) is not the best choice of denaturant for studying a folding reaction. There is an ample amount of evidence to suggest that the variations in the ionic strength (with GdnHCl being an ionic compound) can lead to unexpected effects (2), including an increase in protein stability at low denaturant concentration (3⇓⇓–6) and changes in apparent kinetics of folding …

Reply to Candel et al.: Evidence for evolutionary conservation of folding kinetics in the thioredoxin protein family