Cover Image, Volume 35, Issue 8
Article first published online: 18 FEB 2014
Copyright © 2013 Wiley Periodicals, Inc.
Journal of Computational Chemistry
Volume 35, Issue 8, pages iii–iv, 30 March 2014
How to Cite
(2014), Cover Image, Volume 35, Issue 8. J. Comput. Chem., 35: iii–iv. doi: 10.1002/jcc.23567
- Issue published online: 18 FEB 2014
- Article first published online: 18 FEB 2014
- Cited By
Tryptophan, an essential amino acid, exists in a number of conformations and adopts cationic, anionic, and zwitterionic forms at various pH values. On page 595, Uppula Purushotham and G. Narahari Sastry report a comprehensive computational analysis using DFT, dispersion-corrected DFT, and MP2 methods, quantifying the role played by various noncovalent interactions that impart stability to tryptophan dimers. They also analyze dimers of tryptophan residues in Protein Data Bank (PDB) structures. The cover depicts the various ionic forms of tryptophan and selected orientations of tryptophan dimers obtained from the PDB.