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/

Zendy Pro

Presents the zaia usage as premium feature

ZAIA

Presents AI Discovery search usage as a premium feature

AI Discovery

Presents AI Discovery explain and summary usage as a premium feature

Content Analysis

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Presents the pdf analysis as premium feature

PDF Analysis

1500 Top-up

3000 Top-up

Zendy Basic

2500 Top-up

Zendy Unlimited

Presents the access of premium content as premium feature

Premium Content

The folding of protein into their compact three dimensional structures has enabled living organisms to develop astonishing diversity and selectivity in their underlying chemical processes generating biological activity, the trafficking of molecules to specific cellular locations and the regulation of cellular growth and differentiation. All these processes require long term stability of proteins and only correctly folded proteins possess this attribute. This study has investigated the effect of glucose on thermal stability of myoglobin. We monitored the heme protein interaction at 409 nm and polypeptide backbone at 222 nm. It seems that the glucose molecule is stabilizing protein heme interaction while destabilising overall peptide backbone.

Effect of Glucose on Thermal Stability of Myoglobin: A Biophysical and In silico Approach towards Stabilisation of Protein