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Issue 19, 2008
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Thermodynamics of stacking interactions in proteins

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Using a database of 6166 experimental structures taken from the Protein Data Bank, we have studied pair interactions between planar residues (Phe, Tyr, His, Arg, Glu and Asp) in proteins, known as π–π interactions. On the basis of appropriate coordinates defining the mutual arrangement of two residues, we have calculated 2-D potentials of mean force aimed at determining the stability of the most probable structures for aromatic–aromatic, aromatic–cation and aromatic–anion bound pairs. Our analysis reveals the thermodynamic relevance and the ubiquity of stacked complexes in proteins.

Graphical abstract: Thermodynamics of stacking interactions in proteins

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Supplementary files

Article information

29 Nov 2007
28 Mar 2008
First published
09 Apr 2008

Phys. Chem. Chem. Phys., 2008,10, 2673-2685
Article type

Thermodynamics of stacking interactions in proteins

S. Marsili, R. Chelli, V. Schettino and P. Procacci, Phys. Chem. Chem. Phys., 2008, 10, 2673
DOI: 10.1039/B718519G

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