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. 2019 Jun 17;24(12):2258. doi: 10.3390/molecules24122258

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© 2019 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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Secondary structure and oligomerization status determination of AtNRP2. (a) The near-UV Circular dichroism (CD) spectroscopy profile of full-length AtNRP2 and AtNRP2 NT/CT, showing them to be predominantly α-helical in composition. (b) Analytical gel-filtration chromatogram of full-length AtNRP2 and AtNRP2 NT/CT. The elution volumes obtained were nearly 12.9 and 14.0 mL, respectively, which correspond to the sizes bigger than those of the dimers. (c) Sedimentation velocity analytical ultra-centrifugation of AtNRP2 (left panel) and AtNRP2 NT/CT (middle panel). (d) The plot shows the fitting on c(s) analysis and the distribution of sedimentation coefficients for both the proteins respectively (right panel). Peaks in blue represent full-length AtNRP2 and peaks in purple represent AtNRP2 NT/CT. The higher ‘s’ value corresponds to bigger molecules.