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\begin{document}

\title{Statistical analysis of aromatic interactions in globular proteins}



\author[1]{Mikhail  Lobanov}%
\author[1]{Leonid Pereyaslavets}%
\author[2]{Ilya Likhachev}%
\author[3]{Bakhyt Matkarimov}%
\author[1]{Oxana Galzitskaya}%
\affil[1]{Institute of Protein Research}%
\affil[2]{Institute of Mathematical Problems of Biology}%
\affil[3]{Nazarbayev University}%


\vspace{-1em}



  
  \date{May 25, 2024}


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\selectlanguage{english}
\begin{abstract}
The clustering of protein structures from the Protein Data Bank (PDB)
was performed. The analysis of the conformation of interacting aromatic
residues was carried out for 511 282 pairs in 35 493 protein structures
with 50\% identity. In proteins, pairs with parallel arrangement of
aromatic residues make up 6.2\% of all possible ones, which is twice as
much as expected, pairs with perpendicular arrangement of aromatic
residues make up 25\%. We have demonstrated that 60\selectlanguage{ngerman}° is the most
favorable arrangement of aromatic residues in pairs, as in proteins, and
for an exhaustive enumeration of all conformations of aromatic residues
in pairs. Among all possible aromatic pairs, the His-His pair is found
in proteins twice as often as the expected frequency of the pairs, and
the His-Phe pair turned out to be less than expected one. A server (CARP
-- Contacts of Aromatic Residues in Proteins) has been created for
calculating the general parameters/properties of interacting aromatic
residues in globular proteins
http://bioproteom.protres.ru/arom\_q\_prog/.%
\end{abstract}\selectlanguage{ngerman}%



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\textbf{Hosted file}

\verb`Aromatics_11_05_2021_proteins.docx`  available at \url{https://authorea.com/users/436798/articles/710141-statistical-analysis-of-aromatic-interactions-in-globular-proteins}

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