Title of article :
C-h⋯π-interactions in proteins
Author/Authors :
Maria Brandl، نويسنده , , Manfred S. Weiss، نويسنده , , Andreas Jabs، نويسنده , , Jürgen Sühnel، نويسنده , , Rolf Hilgenfeld، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2001
Abstract :
C-H⋯π-interactions involving aromatic groups either as donor or as acceptor groups are found mostly in the interior of the protein. The more hydrophilic the participating groups are, the closer to the surface are the interactions located.
About 40 % of all C-H⋯π-interactions occur between amino acid residue side-chains that are separated by nine or less residues in sequence. Dependent on the interaction class, different preferences for secondary structure, residue type and side-chain conformation were observed.
It is likely that the C-H⋯π-interactions contribute significantly to the overall stability of a protein.
Keywords :
Hydrogen bond , protein structure , C-H??-interaction , protein stability , force fields
Journal title :
Journal of Molecular Biology
Journal title :
Journal of Molecular Biology