pairing is much more highly conserved than sequence. Distant relationships between proteins whose primary structures are unalignable can sometimes be found by secondary structure. It has been shown that α-helices are more stable, robust to mutations and designable than β-strands in natural proteins, thus designing functional all-α proteins is likely to be easier that designing proteins with both helices and strands; this has been recently confirmed experimentally. See also Folding (chemistry) Nucleic acid secondary structure Translation Structural motif Protein circular dichroism data bank WHAT IF software List of protein secondary structure prediction programs References Further reading (The original beta-sheet conformation article.) (alpha- and pi-helix conformations, since they predicted that helices would not be possible.) External links NetSurfP – Secondary Structure and Surface Accessibility predictor PROF ScrewFit PSSpred A multiple neural network training program for protein secondary structure prediction Genesilico metaserver Metaserver which allows to run over 20 different secondary structure predictors by one click SST webserver: An information-theoretic (compression-based) secondary structural assignment. Protein structure 2 Stereochemistry