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. 2019 Jun 10;9:8383. doi: 10.1038/s41598-019-44413-x

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© The Author(s) 2019

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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Spectral characterization of HCV p7 isolates. (A) 2D ¹H-¹⁵N HSQC spectra of p7(1b/J4) in Cyclofos-6 (left), and p7(5a/EUH1480) in DPC (right), with amino acid assignments indicated. The amino acid assignments of the p7(5a/EUH1480) spectrum were transferred from²⁹. The amino acid sequences of the constructs are shown below the spectra. Below the sequence for p7(5a/EUH1480) are indicated the native amino acids that were substituted in this construct used for experiments here and in²⁹. (B) Top: ¹³Cα secondary chemical shift index for p7(1b/J4) (filled bars) and p7(5a/EUH1480) (open bars), with positive values indicative of α-helical conformation. Bottom: TALOS-N⁴⁶ chemical shift-based secondary structure prediction for p7(1b/J4)(⚪) and p7(5a/EUH1480) (X). Chemical shift data for p7(5a/EUH1480) were taken from the BioMagResBank entry 19162²⁹. Shown above the plot and indicated by unfilled and filled bars are the helical residues determined for p7(5a/EUH1480) from PDB 2M6X and those predicted from chemical shifts for p7(1b/J4), respectively. (C) Left: Membrane CS-Rosetta-based structure of p7(1b/J4). Right: A single subunit of p7(5a/EUH1480) showing the horseshoe-like conformation in the oligomeric model 2M6X²⁹ is shown for comparison. The structures are shaded from blue (N-terminus) to red (C-terminus) and the residues 34–37 are shown as sticks. The residues at the beginning and end of each helix are indicated.