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Issue 23, 2014
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What are the preferred horizontal displacements of aromatic–aromatic interactions in proteins? Comparison with the calculated benzene–benzene potential energy surface

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Abstract

The data from protein structures from the Protein Data Bank and quantum chemical calculations indicate the importance of aromatic–aromatic interactions at large horizontal displacements (offsets). The protein stacking interactions of the phenylalanine residue show preference for large offsets (3.5–5.0 Å), while the calculations show substantially strong interactions, of about −2.0 kcal mol−1.

Graphical abstract: What are the preferred horizontal displacements of aromatic–aromatic interactions in proteins? Comparison with the calculated benzene–benzene potential energy surface

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Publication details

The article was received on 22 Oct 2013, accepted on 24 Apr 2014 and first published on 25 Apr 2014


Article type: Communication
DOI: 10.1039/C3CP54474E
Author version available: Download Author version (PDF)
Citation: Phys. Chem. Chem. Phys., 2014,16, 11173-11177
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    What are the preferred horizontal displacements of aromatic–aromatic interactions in proteins? Comparison with the calculated benzene–benzene potential energy surface

    D. B. Ninković, J. M. Andrić, S. N. Malkov and S. D. Zarić, Phys. Chem. Chem. Phys., 2014, 16, 11173
    DOI: 10.1039/C3CP54474E

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