pipath

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

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

Research output: Contribution to journalArticle

12 Citations (Scopus)

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 2006
Externally publishedYes

Fingerprint

Graph theory
Directed graphs
graph theory
Membrane Proteins
Nuclear magnetic resonance
membranes
solid state
proteins
nuclear magnetic resonance

Keywords

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

ASJC Scopus subject areas

  • Molecular Biology
  • Physical and Theoretical Chemistry
  • Spectroscopy
  • Radiology Nuclear Medicine and imaging
  • Condensed Matter Physics

Cite this

pipath : An optimized algorithm for generating α-helical structures from PISEMA data. / Asbury, T.; Quine, J. R.; Achuthan, S.; Hu, J.; Chapman, Michael; Cross, T. A.; Bertram, R.

In: Journal of Magnetic Resonance, Vol. 183, No. 1, 11.2006, p. 87-95.

Research output: Contribution to journalArticle

Asbury, T. ; Quine, J. R. ; Achuthan, S. ; Hu, J. ; Chapman, Michael ; Cross, T. A. ; Bertram, R. / pipath : An optimized algorithm for generating α-helical structures from PISEMA data. In: Journal of Magnetic Resonance. 2006 ; Vol. 183, No. 1. pp. 87-95.
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