title: The nature of intermolecular interactions between aromatic amino acid residues.
abstract: 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.
authors.affiliation: Dipartimento di Chimica, Università di Firenze, Firenze, Italy. procacci@chim.unifi.it
authors.forename: Francesco Luigi
authors.initials: FL
authors.lastname: Gervasio
authors.forename: Riccardo
authors.initials: R
authors.lastname: Chelli
authors.forename: Piero
authors.initials: P
authors.lastname: Procacci
authors.forename: Vincenzo
authors.initials: V
authors.lastname: Schettino
mesh_terms: 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
chemical_list: D024322:Amino Acids, Aromatic; D014443:Tyrosine; D010649:Phenylalanine; D014364:Tryptophan