Issue 19, 2008

Thermodynamics of stacking interactions in proteins

Abstract

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

Supplementary files

Article information

Article type
Paper
Submitted
29 Nov 2007
Accepted
28 Mar 2008
First published
09 Apr 2008

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

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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