%0 Journal Article %1 Marsili2008PiStackingThermodynamics %A Marsili, Simone %A Chelli, Riccardo %A Schettino, Vincenzo %A Procacci, Piero %D 2008 %I The Royal Society of Chemistry %J Phys. Chem. Chem. Phys. %K computational-biology nonbonded-interactions pi-stacking protein %N 19 %P 2673-2685 %R 10.1039/B718519G %T Thermodynamics of stacking interactions in proteins %U http://dx.doi.org/10.1039/B718519G %V 10 %X 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 small pi-small pi 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.

@article{Marsili2008PiStackingThermodynamics, 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 [small pi]-[small pi] 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.}, added-at = {2016-08-19T21:44:26.000+0200}, author = {Marsili, Simone and Chelli, Riccardo and Schettino, Vincenzo and Procacci, Piero}, biburl = {https://www.bibsonomy.org/bibtex/2ce55bb381921684406843617724cb6f0/salotz}, description = {Thermodynamics of stacking interactions in proteins - Physical Chemistry Chemical Physics (RSC Publishing) DOI:10.1039/B718519G}, doi = {10.1039/B718519G}, interhash = {0fd310bd675d85644c0f463b8c565576}, intrahash = {ce55bb381921684406843617724cb6f0}, journal = {Phys. Chem. Chem. Phys.}, keywords = {computational-biology nonbonded-interactions pi-stacking protein}, number = 19, pages = {2673-2685}, publisher = {The Royal Society of Chemistry}, timestamp = {2016-08-19T21:44:26.000+0200}, title = {Thermodynamics of stacking interactions in proteins}, url = {http://dx.doi.org/10.1039/B718519G}, volume = 10, year = 2008 }