The protein coil library: A structural database of nonhelix, nonstrand fragments derived from the PDB

Nicholas C. Fitzkee, Patrick J. Fleming, George D. Rose

Research output: Contribution to journalArticlepeer-review

Abstract

Approximately half the structure of folded proteins is either α-helix or β-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-α-helix and non-β-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.

Original languageEnglish (US)
Pages (from-to)852-854
Number of pages3
JournalProteins: Structure, Function and Genetics
Volume58
Issue number4
DOIs
StatePublished - Mar 1 2005

Keywords

  • Protein conformation
  • Protein structure
  • Random coil
  • Secondary structure
  • Statistical coil

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology

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