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The structure and stability of a mutated yeast phosphoglycerate mutase in which His-181 has been replaced by alanine have been studied. The secondary, tertiary and quaternary structures of the mutant enzyme in the absence of ligands are essentially identical to those of the wild-type enzyme as revealed by c.d., fluorescence and cross-linking studies. The mutant enzyme is slightly less stable than the wild-type enzyme towards denaturation by guanidium chloride (GdnHCl). On addition of cofactor 2,3-bisphosphoglycerate, the wild-type enzyme shows increased stability towards GdnHCl. However, addition of cofactor causes dramatic changes in the structure of the mutant enzyme, leading to dissociation of the tetrameric form to dimeric and monomeric species.

Substitution of His-181 by alanine in yeast phosphoglycerate mutase leads to cofactor-induced dissociation of the tetrameric structure