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\begin{document}

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



\author[1]{Dominique MIAS-LUCQUIN}%
\author[2]{Isaure Chauvot de Beauchêne}%
\affil[1]{LORIA}%
\affil[2]{CNRS}%


\vspace{-1em}



  
  \date{June 14, 2024}


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\begin{abstract}
We explored the Protein Data-Bank (PDB) to collect protein-ssDNA
structures and create a multi-conformational docking benchmark including
both bound and unbound protein structures. Due to ssDNA high flexibility
when not bound, no ssDNA unbound structure is included. For the 143
groups identified as bound-unbound structures of the same protein , we
studied the conformational changes in the protein induced by the ssDNA
binding. Moreover, based on several bound or unbound protein structures
in some groups, we also assessed the intrinsic conformational
variability in either bound or unbound conditions, and compared it to
the supposedly binding-induced modifications. This benchmark is, to our
knowledge, the first attempt made to peruse available structures of
protein -- ssDNA interactions to such an extent, aiming to improve
computational docking tools dedicated to this kind of molecular
interactions.%
\end{abstract}%



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\textbf{Hosted file}

\verb`p_bench.mk2.Proof.odt`  available at \url{https://authorea.com/users/412462/articles/521169-conformational-variability-in-proteins-bound-to-single-stranded-dna-a-new-benchmark-for-new-docking-perspectives}

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