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

We explored the Protein DataBank (PDB) to collect protein-ssDNA structuresand create a multiconformational docking benchmark including both bound andunbound protein structures. Due to ssDNA high flexibility when not bound, nossDNA unbound structure is included in the benchmark. For the 91sequence-identity groups identified as bound-unbound structures of the sameprotein, we studied the conformational changes in the protein induced by thessDNA binding. Moreover, based on several bound or unbound protein structuresin some groups, we also assessed the intrinsic conformational variability ineither bound or unbound conditions, and compared it to the supposedlybinding-induced modifications. To illustrate a use case of this benchmark, weperformed docking experiments using ATTRACT docking software. This benchmarkis, to our knowledge, the first one made to peruse available structures ofssDNA-protein interactions to such an extent, aiming to improve computationaldocking tools dedicated to this kind of molecular interactions.

Conformational variability in proteins bound to single-stranded DNA: a new benchmark for new docking perspectives