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

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.