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 aim of investigating protein interaction between Homo sapiens adenovirus and heat shock 70 kDa protein (Hsp70) is to study a potentially synergistic interaction that would enhance the anti-apoptotic mechanisms, hence increasing the virus replication rate and improve the killing efficiency of tumour cells in cancer therapy. Currently, the protein interaction between Hsp70 and E1A 32 kDa of human adenovirus C serotype 5 (Ad5) is still unknown. Mutant models (T11V, T12P and D364S) were built, simulated and their interactions with Ad5 were studied. The E1A 32 kDa of human Ad5 motif (PNLVP) showed the lowest binding energy and intermolecular energy values with the novel T11V mutant at -8.26 kcal/mol and -11.21 kcal/mol. The protein-ligand complex models revealed that the T11V mutant had the strongest and most stable interaction with the PNLVP motif among all the four protein-ligand complex structures. This knowledge would assist future in vivo investigations of this protein-ligand complex structure in cancer treatment research.

biologia

Molecular dynamics simulation and docking studies on novel mutants (T11V, T12P and D364S) of the nucleotide-binding domain of human heat shock 70 kDa protein