The edgewise interactions of anions with phenylalanine (Phe) aromatic rings in proteins,
known as anion–quadrupole interactions, have been well studied. However, the anion …

Apparent electrostatics‐defying clustering of arginines attributed as screening effect of
solvent is in this study examined as a possible thermodynamic driving force in protein …

Noncovalent interactions are quite important in biological structure− function relationships.
To study the pairwise interaction of aromatic amino acids (phenylalanine, tyrosine …

The dynamics of anion–quadrupole (or anion− π) interactions formed between negatively
charged (Asp/Glu) and aromatic (Phe) side chains are for the first time computationally …

Cation–π interactions of aromatic rings and positively charged groups are among the most
important interactions in structural biology. The role and energetic characteristics of these …

Weak molecular interactions play an important role in protein structure and function.
Computational tools that identify weak molecular interactions are, therefore, valuable for the …

We have studied the cation–π interactions of neutral aromatic ligands with the cationic
amino acid residues arginine, histidine and lysine using ab initio calculations, symmetry …

Arginine is an abundant residue in protein–protein interfaces. The importance of this residue
relates to the versatility of its side chain in intermolecular interactions. Different classes of …

Cation-π interactions between an aromatic ring and a positive charge located above it have
proven to be important in protein structures and biomolecule associations. Here, the role of …

Protein structures are stabilized using noncovalent interactions. In addition to the traditional
noncovalent interactions, newer types of interactions are thought to be present in proteins …