What are the preferred horizontal displacements of aromatic–aromatic interactions in proteins? Comparison with the calculated benzene–benzene potential energy surface

Literature Information

Publication Date 2014-04-25
DOI 10.1039/C3CP54474E
Impact Factor 3.676
Authors

Dragan B. Ninković, Jelena M. Andrić, Saša N. Malkov


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Abstract

The data from protein structures from the Protein Data Bank and quantum chemical calculations indicate the importance of aromatic–aromatic interactions at large horizontal displacements (offsets). The protein stacking interactions of the phenylalanine residue show preference for large offsets (3.5–5.0 Å), while the calculations show substantially strong interactions, of about −2.0 kcal mol−1.

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Physical Chemistry Chemical Physics

Physical Chemistry Chemical Physics
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Physical Chemistry Chemical Physics (PCCP) is an international journal co-owned by 19 physical chemistry and physics societies from around the world. This journal publishes original, cutting-edge research in physical chemistry, chemical physics and biophysical chemistry. To be suitable for publication in PCCP, articles must include significant innovation and/or insight into physical chemistry; this is the most important criterion that reviewers and Editors will judge against when evaluating submissions. The journal has a broad scope and welcomes contributions spanning experiment, theory, computation and data science. Topical coverage includes spectroscopy, dynamics, kinetics, statistical mechanics, thermodynamics, electrochemistry, catalysis, surface science, quantum mechanics, quantum computing and machine learning. Interdisciplinary research areas such as polymers and soft matter, materials, nanoscience, energy, surfaces/interfaces, and biophysical chemistry are welcomed if they demonstrate significant innovation and/or insight into physical chemistry. Joined experimental/theoretical studies are particularly appreciated when complementary and based on up-to-date approaches.

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