title: Conformational and geometrical properties of idealized beta-barrels in proteins.
abstract: An equation for calculating the distances between the atoms involved in forming an idealized hydrogen bond in a parallel or antiparallel beta-barrel has been derived by adjusting the corresponding data given by Pauling and Corey for a beta-sheet. Based on these distances, a geometrical optimization method was developed, by which one can generate various idealized beta-barrels: parallel or antiparallel, tilted or non-tilted, right-tilted or left-tilted. For each type of idealized beta-barrel thus obtained, the corresponding conformation and characteristic geometric parameters as well as their relationship are analyzed and discussed. Since the strand in a tilted beta-barrel traces a curve rather than a straight line on a cylinder-like surface, a regular chain in which the dihedral angles of each residue are the same cannot form a tilted beta-barrel but only a non-tilted beta-barrel. As observed, the strands of a right-tilted beta-barrel possess a very strong right-handed twist. The radii of the idealized tilted parallel and antiparallel beta-barrels are greater than those of the corresponding non-tilted ones by approximately 1 A and approximately 1.5 A, respectively. Consequently, there is relatively more room for a tilted beta-barrel to accommodate the internal side-chains, suggesting that a conformational change from a non-tilted beta-barrel to a tilted one would ease the repulsion among the crowded internal side-chains so as to make the structure more stable. The values of root-mean-square fits indicate that the idealized right-tilted beta-barrels coincide quite well with the observed beta-barrels in both parallel and antiparallel cases.
authors.affiliation: Computational Chemistry, Upjohn Research Laboratories, Kalamazoo, MI 49001.
authors.forename: K C
authors.initials: KC
authors.lastname: Chou
authors.forename: L
authors.initials: L
authors.lastname: Carlacci
authors.forename: G M
authors.initials: GM
authors.lastname: Maggiora
authors.forename: G G
authors.initials: GG
authors.lastname: Maggiora
mesh_terms: D055598:Chemical Phenomena; D002627:Chemistry, Physical; D006860:Hydrogen Bonding; D015394:Molecular Structure; D011487:Protein Conformation; D011506:Proteins
chemical_list: D011506:Proteins