Foldon domain explained

Foldon domain is a small, approximately 30 amino acid, protein domain originally discovered on the fibritin protein of bacteriophage T4. The domain causes proteins to trimerize and is used in several biotechnology and vaccine applications.[1] [2] [3] [4] [5]

Notes and References

  1. Meier. Sebastian. 3 December 2004. Foldon, the natural trimerization domain of T4 fibritin, dissociates into a monomeric A-state form containing a stable beta-hairpin: atomic details of trimer dissociation and local beta-hairpin stability from residual dipolar couplings. Journal of Molecular Biology. 344. 4. 1051–1069. 10.1016/j.jmb.2004.09.079. 15544812 . 15 August 2024.
  2. Rutten. Lucy. 8 March 2024. Foldon, the natural trimerization domain of T4 fibritin, dissociates into a monomeric A-state form containing a stable beta-hairpin: atomic details of trimer dissociation and local beta-hairpin stability from residual dipolar couplings. Nature. 14. 1. 5735 . 10.1038/s41598-024-56293-x. 38459086 . 10923862 .
  3. Wang. Xinzhe. 2017. Oligomerization triggered by foldon: a simple method to enhance the catalytic efficiency of lichenase and xylanase. BMC Biotechnology. 17. 10.1186/s12896-017-0380-3. free . 5496177.
  4. Web site: Disulfide-linked Foldon Domains To Stabilize Protein Trimers. Stanford University. 15 August 2024.
  5. Lu. Yuan. 15 November 2013. Production and stabilization of the trimeric influenza hemagglutinin stem domain for potentially broadly protective influenza vaccines . PNAS. 111. 1. 125–130. 10.1073/pnas.1308701110. free . 24344259 . 3890838 .

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