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. 2017 Jul 11;7:5158. doi: 10.1038/s41598-017-05328-7

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© The Author(s) 2017

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Unfolding forces of LHCII depend on trimerization and the lipid matrix. (a) Multivariate kernel density estimate of the unfolding force as a function of the contour length for LHCII monomers in POPG (top right) and LHCII trimers in POPG (top left), pure DGDG (bottom left) and a mixture of DGDG and MGDG (bottom right). The dots mark the most likely unfolding forces for a given contour length, while the diameter of the dots represents their relative probability of at least 40% in relation to the most probable unfolding event. The histograms (grey) at the axes show the individual underlying distributions of unfolding forces and contour lengths. (b) Most likely unfolding force as a function of the contour length (obtained from the dots in (a)) as a function of oligomerization state (top) and lipid mixture (bottom). Helices (H1-5) are indicated as shaded gray areas. The color shaded areas indicate the standard error of the most likely unfolding force. The trimer shows enhanced stabilization compared to the monomer in distinct domains of the protein, indicated by numbers 1 to 5. Both glycolipids provide additional stability for trimeric LHCII at helix 4, while the addition of MGDG strongly increases the unfolding forces in many segments along the LHCII polypeptide.