title: Ideal architecture of residue packing and its observation in protein structures.
abstract: A simple model of sphere packing has been investigated as an ideal model for long-range interactions for the packing of non-bonded residues in protein structures. By superposing all residues, the geometry of packing around a central residue is investigated. It is found that all residues conform almost perfectly to this lattice model for sphere packing when a radius of 6.5 A is used to define non-bonded (virtual) interacting residues. Side-chain positions with respect to sequential backbone segments are relatively regular as well. This lattice can readily be used in conformation simulations to reduce the conformational space.
authors.affiliation: Molecular Structure Section, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892-5677, USA.
authors.forename: G
authors.initials: G
authors.lastname: Raghunathan
authors.forename: R L
authors.initials: RL
authors.lastname: Jernigan
mesh_terms: D000596:Amino Acids / Q000737:chemistry; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D008958:Models, Molecular; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*
chemical_list: D000596:Amino Acids; D011506:Proteins