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You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue.
Introduction to Miraculin
Miracle? I think you mean Miraculin.
Miraculin is a protein that is best known for its ability to deceive human taste buds into thinking
sour or acidic food is sweet. This homodimeric glycoprotein was first identified in the West
African native fruit, Synsepalum dulcificum (also known as “Miracle Fruit”), and exists in the
pulp of the miracle fruit.
Miraculin’s deceptive properties have been exploited by several companies as sugar substitutes.
However, the American Food and Drug Administration banned the use of miraculin after
labeling it as an additive [3] . This
prevented its commercial use in the food industry.
Miraculin’s Structure
Miraculin is composed of 191 amino acid residues linked primarily by peptide bonds,
having a molecular weight of about 28 kDa. Sarroch Theerasil et al [4] use HPLC profiles and SDS-PAGE
analyses to prove this.
Miraculin is a homodimer made by two chains that have two N-glycosylated Asn residues and
are cross-linked through a disulfide bridge. Miraculin can also exist in a tetramer form.
Predictivley-modeled structure of miraculin
test
Miraculin’s interactions with human tongue receptors
test
Miraculin-Like Proteins (MLPs)
Several miraculin-like proteins (MLPs) have been identified and are classified as
“miraculin-like” based on amino-acid sequence alignment with that of miraculin. MLPs and
miraculin are categorized into the Kunitz-type soybean trypsin inhibitor (STI) family. Features
common to the Kunitz-type soybean trypsin inhibitor (STI) family include the presence of
disulfide bridges --which are apparent in miraculin models-- and the inhibition of trypsin and
chymotrypsin. Examples include MLPs extracted from Murraya koenigii and Vitis vinifera plants.
Since atomic-level structural data of miraculin is not available to date, a miraculin-like protein
(MLP) homologous to miraculin extracted from Murraya koenigii will be used for protein
visualization purposes.
FILL IN
Other Proteins with Function Similar to Miraculin
Although miraculin-like proteins have already been discussed, the title of being “like” miraculin
comes from its structural identity to miraculin rather than its functional identity.
Neoculin (also goes by the name “curculin”) is another protein that “tricks” tongue receptors into
perceiving sour taste as sweet. This protein is native to the Malaysian fruit of Curculigo latifolia.
Unlike miraculin, neoculin is not tasteless and instead has a sweet taste on its own. Like
miraculin though, the active form of neoculin is heterodimer consisting of two moners that are
connected through disulfide bridges . [5]
Thaumatin is another protein with taste-modifying properties. Like miraculin, this protein is also
extracted from a plant native to West Africa. Thaumatin is a sweet tasting-protein with the ability
to enhance the tongue’s response to sweet taste by more than 100 fold [6].
References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
- ↑ https://www.accessdata.fda.gov/cms_ia/importalert_120.html
- ↑
https://www.jbc.org/content/263/23/11536.full.pdf+html
- ↑ https://doi.org/10.1016/j.febslet.2004.07.073
- ↑
https://doi.org/10.1159/000059716
