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Issue 43, 2014
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What are preferred water–aromatic interactions in proteins and crystal structures of small molecules?

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Abstract

The distribution of water molecules around aromatic rings in the protein structures and crystal structures of small molecules shows quite a small number of the strongest OH–π interactions, a larger number of parallel interactions, and the largest number of the weakest CH–O interactions.

Graphical abstract: What are preferred water–aromatic interactions in proteins and crystal structures of small molecules?

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Publication details

The article was received on 04 Mar 2014, accepted on 15 Sep 2014 and first published on 17 Sep 2014


Article type: Communication
DOI: 10.1039/C4CP00929K
Author version available: Download Author version (PDF)
Citation: Phys. Chem. Chem. Phys., 2014,16, 23549-23553
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    What are preferred water–aromatic interactions in proteins and crystal structures of small molecules?

    G. V. Janjić, S. N. Malkov, M. V. Živković and S. D. Zarić, Phys. Chem. Chem. Phys., 2014, 16, 23549
    DOI: 10.1039/C4CP00929K

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