PIPATH: an optimized algorithm for generating alpha-helical structures from PISEMA data.
An optimized algorithm for finding structures and assignments of solid-state NMR PISEMA data obtained from alpha-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.
Asbury
T
T
Institute of Molecular Biophysics, Florida State University, Tallahassee, FL 32306, USA.
Quine
J R
JR
Achuthan
S
S
Hu
J
J
Chapman
M S
MS
Cross
T A
TA
Bertram
R
R
D000465:Algorithms; D003198:Computer Simulation; D003461:Crystallography; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008565:Membrane Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D008956:Models, Chemical; D008958:Models, Molecular; D017433:Protein Structure, Secondary; D013113:Spin Labels
D008565:Membrane Proteins; D013113:Spin Labels