title: On alpha-helices terminated by glycine. 1. Identification of common structural features.
abstract: About one third of all helices is terminated by residues with a positive torsion angle phi. 74% of them are glycines. This strong propensity can be explained by typical bifurcated three-center hydrogen bonds which are only compatible with a positive torsion angle phi, causing helix termination. An algorithm was developed to identify these structural features in alpha-helices. 158 out of 456 helices in 79 different well-refined protein structures examined in our analysis were found to have a glycine with this special conformation which have been conserved remarkably during evolution.
authors.affiliation: Charité, Humboldt Universität, Institut für Biochemie, Berlin, Germany.
authors.forename: R
authors.initials: R
authors.lastname: Preissner
authors.forename: P
authors.initials: P
authors.lastname: Bork
mesh_terms: D000465:Algorithms; D016206:Databases, Bibliographic; D005998:Glycine; D006860:Hydrogen Bonding; D008958:Models, Molecular; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry
chemical_list: D011506:Proteins; D005998:Glycine