Foldon domain: Difference between revisions
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'''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 [[oligomerization|trimerize]] and is used in several [[biotechnology]] and [[vaccine]] applications.<ref>{{cite journal |last1=Meier|first1=Sebastian|date=3 December 2004|title=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|url=https://pubmed.ncbi.nlm.nih.gov/15544812/|journal=[[Journal of Molecular Biology]]|volume= 344|issue= 4|pages= 1051–1069|doi=10.1016/j.jmb.2004.09.079|pmid=15544812 |access-date=15 August 2024}}</ref><ref>{{cite journal |last1=Rutten|first1=Lucy|date=8 March 2024|title=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=[[Nature]]|volume= 14|issue= 1|page=5735 |doi=10.1038/s41598-024-56293-x|pmid=38459086 |pmc=10923862 }}</ref><ref>{{cite journal |last1=Wang|first1=Xinzhe|date= 2017|title=Oligomerization triggered by foldon: a simple method to enhance the catalytic efficiency of lichenase and xylanase|journal=[[BMC Biotechnology]]|volume= 17|issue= |pages= |doi=10.1186/s12896-017-0380-3|doi-access=free |pmc=5496177}}</ref><ref>{{cite web |url=https://techfinder.stanford.edu/technology/disulfide-linked-foldon-domains-stabilize-protein-trimers|title=Disulfide-linked Foldon Domains To Stabilize Protein Trimers|last= |first= |date= |website= |publisher=[[Stanford University]]|access-date=15 August 2024|quote=}}</ref><ref>{{cite journal |last1=Lu|first1=Yuan|date=15 November 2013|title=Production and stabilization of the trimeric influenza hemagglutinin stem domain for potentially broadly protective influenza vaccines |journal=[[PNAS]]|volume= 111|issue= 1|pages= 125–130|doi=10.1073/pnas.1308701110|doi-access=free |pmid=24344259 |pmc=3890838 }}</ref> |
'''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 [[oligomerization|trimerize]] and is used in several [[biotechnology]] and [[vaccine]] applications.<ref>{{cite journal |last1=Meier|first1=Sebastian|date=3 December 2004|title=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|url=https://pubmed.ncbi.nlm.nih.gov/15544812/|journal=[[Journal of Molecular Biology]]|volume= 344|issue= 4|pages= 1051–1069|doi=10.1016/j.jmb.2004.09.079|pmid=15544812 |access-date=15 August 2024}}</ref><ref>{{cite journal |last1=Rutten|first1=Lucy|date=8 March 2024|title=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=[[Nature (journal)|Nature]]|volume= 14|issue= 1|page=5735 |doi=10.1038/s41598-024-56293-x|pmid=38459086 |pmc=10923862 }}</ref><ref>{{cite journal |last1=Wang|first1=Xinzhe|date= 2017|title=Oligomerization triggered by foldon: a simple method to enhance the catalytic efficiency of lichenase and xylanase|journal=[[BMC Biotechnology]]|volume= 17|issue= |pages= |doi=10.1186/s12896-017-0380-3|doi-access=free |pmc=5496177}}</ref><ref>{{cite web |url=https://techfinder.stanford.edu/technology/disulfide-linked-foldon-domains-stabilize-protein-trimers|title=Disulfide-linked Foldon Domains To Stabilize Protein Trimers|last= |first= |date= |website= |publisher=[[Stanford University]]|access-date=15 August 2024|quote=}}</ref><ref>{{cite journal |last1=Lu|first1=Yuan|date=15 November 2013|title=Production and stabilization of the trimeric influenza hemagglutinin stem domain for potentially broadly protective influenza vaccines |journal=[[PNAS]]|volume= 111|issue= 1|pages= 125–130|doi=10.1073/pnas.1308701110|doi-access=free |pmid=24344259 |pmc=3890838 }}</ref> |
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==References== |
==References== |
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Latest revision as of 15:38, 18 October 2024
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]
References
[edit]- ^ 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. doi:10.1016/j.jmb.2004.09.079. PMID 15544812. Retrieved 15 August 2024.
- ^ 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. doi:10.1038/s41598-024-56293-x. PMC 10923862. PMID 38459086.
- ^ Wang, Xinzhe (2017). "Oligomerization triggered by foldon: a simple method to enhance the catalytic efficiency of lichenase and xylanase". BMC Biotechnology. 17. doi:10.1186/s12896-017-0380-3. PMC 5496177.
- ^ "Disulfide-linked Foldon Domains To Stabilize Protein Trimers". Stanford University. Retrieved 15 August 2024.
- ^ 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. doi:10.1073/pnas.1308701110. PMC 3890838. PMID 24344259.