title: Calibration of effective van der Waals atomic contact radii for proteins and peptides.
abstract: Effective van der Waals radii were calibrated in such a way that molecular models built from standard bond lengths and bond angles reproduced the amino acid conformations observed by crystallography in proteins and peptides. The calibrations were based on the comparison of the Ramachandran plots prepared from high-resolution X-ray data of proteins and peptides with the allowed phi, psi torsional angle space for the dipeptide molecular models. The calibrated radii are useful as criteria with which to filter energetically improbable conformations in molecular modeling studies of proteins and peptides.
authors.affiliation: Department of Pharmacology, Washington University School of Medicine, St. Louis, Missouri 63110.
authors.forename: H
authors.initials: H
authors.lastname: Iijima
authors.forename: J B
authors.initials: JB
authors.lastname: Dunbar
authors.forename: G R
authors.initials: GR
authors.lastname: Marshall
mesh_terms: D055598:Chemical Phenomena; D002627:Chemistry, Physical; D010455:Peptides; D011487:Protein Conformation
chemical_list: D010455:Peptides