What are the preferred horizontal displacements of aromatic–aromatic interactions in proteins? Comparison with the calculated benzene–benzene potential energy surface-Reference-Cited by-同舟云学术

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

Published:2014 Issue:23 Volume:16 Page:11173-11177
ISSN:1463-9076
Container-title:Phys. Chem. Chem. Phys.
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Ninković Dragan B.¹²,Andrić Jelena M.¹²,Malkov Saša N.³⁴²,Zarić Snežana D.⁵⁴²⁵⁶

Affiliation:

1. Innovation center of the Department of Chemistry

2. 11000 Belgrade, Serbia

3. Department of Mathematics

4. University of Belgrade

5. Department of Chemistry

6. Texas A & M University at Qatar

Abstract

Stacking interactions of phenylalanine residues show preference for large offsets (3.5–5.0 Å), while the calculations show substantially strong interactions, of about −2.0 kcal mol⁻¹.

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://pubs.rsc.org/en/content/articlepdf/2014/CP/C3CP54474E

Reference51 articles.

1. Aromatic Rings in Chemical and Biological Recognition: Energetics and Structures

2. A Medicinal Chemist’s Guide to Molecular Interactions

3. Aromatic−Aromatic Interactions Induce the Self-Assembly of Pentapeptidic Derivatives in Water To Form Nanofibers and Supramolecular Hydrogels

4. Introducing Quadrupole Interactions into the Peptide Design Toolkit

5. Binding Mechanisms in Supramolecular Complexes

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