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Structure of Haze Forming Proteins in White Wines: Vitis vinifera Thaumatin-Like Proteins

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 o...

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Autores principales: Marangon, Matteo, Van Sluyter, Steven C., Waters, Elizabeth J., Menz, Robert I.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4252030/
https://www.ncbi.nlm.nih.gov/pubmed/25463627
http://dx.doi.org/10.1371/journal.pone.0113757
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author Marangon, Matteo
Van Sluyter, Steven C.
Waters, Elizabeth J.
Menz, Robert I.
author_facet Marangon, Matteo
Van Sluyter, Steven C.
Waters, Elizabeth J.
Menz, Robert I.
author_sort Marangon, Matteo
collection PubMed
description 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°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.
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spelling pubmed-42520302014-12-05 Structure of Haze Forming Proteins in White Wines: Vitis vinifera Thaumatin-Like Proteins Marangon, Matteo Van Sluyter, Steven C. Waters, Elizabeth J. Menz, Robert I. PLoS One Research Article 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°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. Public Library of Science 2014-12-02 /pmc/articles/PMC4252030/ /pubmed/25463627 http://dx.doi.org/10.1371/journal.pone.0113757 Text en © 2014 Marangon et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Marangon, Matteo
Van Sluyter, Steven C.
Waters, Elizabeth J.
Menz, Robert I.
Structure of Haze Forming Proteins in White Wines: Vitis vinifera Thaumatin-Like Proteins
title Structure of Haze Forming Proteins in White Wines: Vitis vinifera Thaumatin-Like Proteins
title_full Structure of Haze Forming Proteins in White Wines: Vitis vinifera Thaumatin-Like Proteins
title_fullStr Structure of Haze Forming Proteins in White Wines: Vitis vinifera Thaumatin-Like Proteins
title_full_unstemmed Structure of Haze Forming Proteins in White Wines: Vitis vinifera Thaumatin-Like Proteins
title_short Structure of Haze Forming Proteins in White Wines: Vitis vinifera Thaumatin-Like Proteins
title_sort structure of haze forming proteins in white wines: vitis vinifera thaumatin-like proteins
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4252030/
https://www.ncbi.nlm.nih.gov/pubmed/25463627
http://dx.doi.org/10.1371/journal.pone.0113757
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