Editing Silent mutation (section)

=== Tertiary structure ===
{{main|Biomolecular structure#Tertiary structure}}
Silent mutations affect protein folding and function.<ref name="pmid17185560"/>  Normally a misfolded protein can be refolded with the help of molecular chaperones. RNA typically produces two common misfolded proteins by tending to fold together and become stuck in different conformations and it has a difficulty singling in on the favored specific tertiary structure because of other competing structures.  RNA-binding proteins can assist RNA folding problems, however, when a silent mutation occurs in the mRNA chain, these chaperones do not bind properly to the molecule and are unable to redirect the mRNA into the correct fold.<ref>{{cite journal | vauthors = Herschlag D | title = RNA chaperones and the RNA folding problem | journal = The Journal of Biological Chemistry | volume = 270 | issue = 36 | pages = 20871–4 | date = September 1995 | pmid = 7545662 | doi = 10.1074/jbc.270.36.20871 | citeseerx = 10.1.1.328.5762 | s2cid = 14083129 | doi-access = free }}</ref>

Recent research suggests that silent mutations can have an effect on subsequent protein structure and activity.<ref>{{cite journal | vauthors = Komar AA | title = Genetics. SNPs, silent but not invisible | journal = Science | volume = 315 | issue = 5811 | pages = 466–7 | date = January 2007 | pmid = 17185559 | doi = 10.1126/science.1138239 | s2cid = 41904137 | doi-access = free }}</ref><ref>{{cite web |author=Beckman |title=The Sound of a Silent Mutation |date=22 December 2006 |work=News |publisher=Science/AAAS |url=https://www.science.org/content/article/sound-silent-mutation}}</ref> The timing and rate of protein folding can be altered, which can lead to functional impairments.<ref name="pmid22577471">{{cite journal | vauthors = Zhang Z, Miteva MA, Wang L, Alexov E | title = Analyzing effects of naturally occurring missense mutations | journal = Computational and Mathematical Methods in Medicine | volume = 2012 | pages = 1–15 | year = 2012 | pmid = 22577471 | pmc = 3346971 | doi = 10.1155/2012/805827 | doi-access = free }}</ref>