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 Plus monthly

Global: Zendy Tools annual

Global: Zendy Tools monthly

Global: Zendy Free Plan

Studying all non-redundant proteins in 76 most-commonly found structuraldomains, the present work attempts to decipher latent patterns thatcharacterize acceptable and unacceptable symmetries in residue-residueinteractions in functional proteins. We report that cutting across thestructural classes, a select set of pairwise interactions are universallyfavored by geometrical and evolutionary constraints, termed 'acceptable'structural and evolutionary tunnels, respectively. An equally small subset ofresidue-residue interactions, the 'unacceptable' structural and evolutionarytunnels, is found to be universally disliked by structural and evolutionaryconstraints. Non-trivial overlapping is detected among acceptable structuraland evolutionary tunnels, as also among unacceptable structural andevolutionary tunnels. A subset of tunnels is found to have equal relativeimportance, structurally and evolutionarily, in different structural classes.The MET-MET tunnel is detected to be universally most unacceptable by bothstructural and evolutionary constraints, whereas the ASP-LEU tunnel was foundto be the closest approximation to be universally most acceptable. Residualpopulations in structural and evolutionary tunnels are found to be independentof stereochemical properties of individual residues. It is argued with examplesthat tunnels are emergent features that connect extent of symmetry inresidue-residue interactions to the level of quaternary structuralorganization.

Structural and evolutionary tunnels of pairwise residue-interaction symmetries connect different structural classes of proteins