Editing Protein secondary structure (section)

== Applications ==

Both protein and nucleic acid secondary structures can be used to aid in [[multiple sequence alignment]]. These alignments can be made more accurate by the inclusion of secondary structure information in addition to simple sequence information. This is sometimes less useful in RNA because base pairing is much more highly conserved than sequence. Distant relationships between proteins whose primary structures are unalignable can sometimes be found by secondary structure.<ref name="Simossis_2004"/>

It has been shown that α-helices are more stable, robust to mutations, and designable than β-strands in natural proteins,<ref>{{cite journal | vauthors = Abrusán G, Marsh JA | title = Alpha Helices Are More Robust to Mutations than Beta Strands | journal = PLOS Computational Biology | volume = 12 | issue = 12 | pages = e1005242 | date = December 2016 | pmid = 27935949 | pmc = 5147804 | doi = 10.1371/journal.pcbi.1005242 | bibcode = 2016PLSCB..12E5242A | doi-access = free }}</ref> 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.<ref>{{cite journal | vauthors = Rocklin GJ, Chidyausiku TM, Goreshnik I, Ford A, Houliston S, Lemak A, Carter L, Ravichandran R, Mulligan VK, Chevalier A, Arrowsmith CH, Baker D | display-authors = 6 | title = Global analysis of protein folding using massively parallel design, synthesis, and testing | journal = Science | volume = 357 | issue = 6347 | pages = 168–175 | date = July 2017 | pmid = 28706065 | pmc = 5568797 | doi = 10.1126/science.aan0693 | bibcode = 2017Sci...357..168R }}</ref>