title: The Protein Coil Library: a structural database of nonhelix, nonstrand fragments derived from the PDB.
abstract: Approximately half the structure of folded proteins is either alpha-helix or beta-strand. We have developed a convenient repository of all remaining structure after these two regular secondary structure elements are removed. The Protein Coil Library (http://roselab.jhu.edu/coil/) allows rapid and comprehensive access to non-alpha-helix and non-beta-strand fragments contained in the Protein Data Bank (PDB). The library contains both sequence and structure information together with calculated torsion angles for both the backbone and side chains. Several search options are implemented, including a query function that uses output from popular PDB-culling servers directly. Additionally, several popular searches are stored and updated for immediate access. The library is a useful tool for exploring conformational propensities, turn motifs, and a recent model of the unfolded state.
authors.affiliation: T. C. Jenkins Department of Biophysics, Johns Hopkins Univeristy, Baltimore, Maryland 21218-2608, USA.
authors.forename: Nicholas C
authors.initials: NC
authors.lastname: Fitzkee
authors.forename: Patrick J
authors.initials: PJ
authors.lastname: Fleming
authors.forename: George D
authors.initials: GD
authors.lastname: Rose
mesh_terms: D000465:Algorithms; D001703:Biophysics / Q000379:methods; D019295:Computational Biology; D030562:Databases, Protein; D015723:Gene Library; D006860:Hydrogen Bonding; D008024:Ligands; D008958:Models, Molecular; D019151:Peptide Library; D011485:Protein Binding; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry; D040901:Proteomics / Q000379:methods; D016415:Sequence Alignment; D017421:Sequence Analysis; D020539:Sequence Analysis, Protein; D012984:Software
chemical_list: D008024:Ligands; D019151:Peptide Library; D011506:Proteins