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

Optical rotatory dispersion and circular dichroism studies reveal that between pH 5 and 7 concana-valin A undergoes a conformational transition which involves a slight loss of fJ-structure but no perturbation of aromatic residues. The dimer-tetramer association of concanavalin A may influence this transition but its contribution is relatively small and difficult to estimate. Near-u.v. circular di-chroism spectra reveal conformational differences between intact and fragmented units of the protein.

A Conformational Transition in Concanavalin A. Conformational Differences between Intact and Fragmented Units