Structural highlights
Function
F6HUG9_VITVI
Publication Abstract from PubMed
Grape thaumatin-like proteins (TLPs) play roles in plant-pathogen interactions and can cause protein haze in white wine unless removed prior to bottling. Different isoforms of TLPs have different hazing potential and aggregation behavior. Here we present the elucidation of the molecular structures of three grape TLPs that display different hazing potential. The three TLPs have very similar structures despite belonging to two different classes (F2/4JRU is a thaumatin-like protein while I/4L5H and H2/4MBT are VVTL1), and having different unfolding temperatures (56 vs. 62 degrees C), with protein F2/4JRU being heat unstable and forming haze, while I/4L5H does not. These differences in properties are attributable to the conformation of a single loop and the amino acid composition of its flanking regions.
Structure of Haze Forming Proteins in White Wines: Vitis vinifera Thaumatin-Like Proteins.,Marangon M, Van Sluyter SC, Waters EJ, Menz RI PLoS One. 2014 Dec 2;9(12):e113757. doi: 10.1371/journal.pone.0113757., eCollection 2014. PMID:25463627[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Marangon M, Van Sluyter SC, Waters EJ, Menz RI. Structure of Haze Forming Proteins in White Wines: Vitis vinifera Thaumatin-Like Proteins. PLoS One. 2014 Dec 2;9(12):e113757. doi: 10.1371/journal.pone.0113757., eCollection 2014. PMID:25463627 doi:http://dx.doi.org/10.1371/journal.pone.0113757
