The nature of intermolecular interactions between aromatic amino acid residues.
The nature of intermolecular interactions between aromatic amino acid residues has been investigated by a combination of molecular dynamics and ab initio methods. The potential energy surface of various interacting pairs, including tryptophan, phenilalanine, and tyrosine, was scanned for determining all the relevant local minima by a combined molecular dynamics and conjugate gradient methodology with the AMBER force field. For each of these minima, single-point correlated ab initio calculations of the binding energy were performed. The agreement between empirical force field and ab initio binding energies of the minimum energy structures is excellent. Aromatic-aromatic interactions can be rationalized on the basis of electrostatic and van der Waals interactions, whereas charge transfer or polarization phenomena are small for all intermolecular complexes and, particularly, for stacked structures. Proteins 2002;48:117-125.
Gervasio
Francesco Luigi
FL
Dipartimento di Chimica, Università di Firenze, Firenze, Italy. procacci@chim.unifi.it
Chelli
Riccardo
R
Procacci
Piero
P
Schettino
Vincenzo
V
D024322:Amino Acids, Aromatic / Q000737:chemistry*; D008958:Models, Molecular; D015394:Molecular Structure; D010649:Phenylalanine / Q000737:chemistry; D055672:Static Electricity; D014364:Tryptophan / Q000737:chemistry; D014443:Tyrosine / Q000737:chemistry
D024322:Amino Acids, Aromatic; D014443:Tyrosine; D010649:Phenylalanine; D014364:Tryptophan