Before revision:  With extensive analysis from varying standpoints we prove here that, such Poisson flows suggest the 3-10-helices and especially Pi-helices to be evidences of nature's mistakes on folding pathways. This hypothesis is further supported by results of critical evolutionary analysis on 20 major protein domain families, which reveal the definitive trend that proteins try to dispose these structures off during evolution, in favor of alpha-helices. Alongside these unexpected and significant results } , a new algorithm to differentiate between related sequences is proposed here that reliably studies evolutionary distance with respect to protein secondary structures.
After revision:  With extensive analysis from varying standpoints we prove here that, such Poisson flows suggest the 3-10-helices and especially Pi-helices revealed that these could be best described by gamma and exponential distributions, across structural classes. Comparative study of normalized percentage of non-glycine and non-proline residues in 3(10), Pi and alpha-helices revealed a considerably higher proportion of 3(10) and Pi-helix residues in disallowed, generous and allowed regions of Ramachandran map. Probe into these findings in the light of evolution suggested clearly that 3(10) and Pi-helices should appropriately be viewed as evolutionary intermediates on long time scale, for not only the } , a new algorithm to differentiate between related sequences is proposed here that reliably studies evolutionary distance with respect to protein secondary structures.