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 Tools annual

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 monthly

Global: Zendy Plus monthly

Presents the access of premium content as premium feature

Premium Content

Global: Zendy Plus annual

Global: Zendy Free Plan

Significance The rate at which proteins accumulate amino acid substitutions during evolution depends on the likelihood that mutations will disrupt structure or affect function. Many mutations affect the ability of proteins to fold correctly, and previous studies showed that the burden imposed by misfolded proteins in cells heavily influences evolutionary rates of proteins. However, these studies could not examine the influence of function on evolutionary rates. The work described here examines the relationship between structural and functional divergence in a rapidly evolving protein family. This analysis revealed that family members that evolved a new function retained more ancestral sequence and structural characteristics, suggesting that the rate of protein evolution is not proportional to the capacity to evolve new functions.

Loss of quaternary structure is associated with rapid sequence divergence in the OSBS family