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

Significance Although novel experimental approaches open exciting opportunities for understanding the elusive protein-folding pathways, interpreting experiments in terms of microscopic folding mechanisms often poses a serious challenge. Here, we demonstrate that extensive sets of global and site-specific unfolding data for two small proteins can be quantitatively explained by a simple statistical–mechanical model derived from known native protein structures. Remarkably, differences in folding between two proteins with similar structures are captured without need to consider sequence-specific interresidue interactions. This finding is significant because it implies that knowledge of the native structure—which implicitly includes sequence information—is sufficient for predicting detailed, site-specific folding mechanisms.

Sequence, structure, and cooperativity in folding of elementary protein structural motifs