pipath: An optimized algorithm for generating α-helical structures from PISEMA data

T. Asbury, J. R. Quine, S. Achuthan, J. Hu, M. S. Chapman, T. A. Cross, R. Bertram

Research output: Contribution to journalArticle

12 Scopus citations

Abstract

An optimized algorithm for finding structures and assignments of solid-state NMR PISEMA data obtained from α-helical membrane proteins is presented. The description of this algorithm, pipath, is followed by an analysis of its performance on simulated PISEMA data derived from synthetic and experimental structures. pipath transforms the assignment problem into a path-finding problem for a directed graph, and then uses techniques of graph theory to efficiently find candidate assignments from a very large set of possibilities.

Original languageEnglish (US)
Pages (from-to)87-95
Number of pages9
JournalJournal of Magnetic Resonance
Volume183
Issue number1
DOIs
StatePublished - Nov 1 2006

Keywords

  • Automated structure determination
  • Membrane proteins
  • PISEMA
  • Solid-state NMR
  • α-Helices

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Nuclear and High Energy Physics
  • Condensed Matter Physics

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    Asbury, T., Quine, J. R., Achuthan, S., Hu, J., Chapman, M. S., Cross, T. A., & Bertram, R. (2006). pipath: An optimized algorithm for generating α-helical structures from PISEMA data. Journal of Magnetic Resonance, 183(1), 87-95. https://doi.org/10.1016/j.jmr.2006.07.020