_tcm18-11426.gif )
An international journal for the fastest publication of high-quality original work in physical chemistry, chemical physics and biophysical chemistry.
Subscribers
Non-subscribers
- Purchase article PDF [£27 + taxes]
- Purchase article PDF member offer [£5 + taxes]
Free access
Paper
Phys. Chem. Chem. Phys., 2008, 10, 2673 - 2685, DOI: 10.1039/b718519g
Thermodynamics of stacking interactions in proteins
Simone Marsili, Riccardo Chelli, Vincenzo Schettino and Piero Procacci
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
– 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.
RSS feed
