Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2021 Feb 11;12:939. doi: 10.1038/s41467-021-21184-6

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© The Author(s) 2021, corrected publication 2021

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/.

PMC Copyright notice

Fig. 3 — a Topological schemes of SBP1_9.a and SBP2_9.a. Coiled-coil pairs are represented as coloured helices, N- and C-termini are indicated with circled letters. b CD spectra of the proteins SBP1_9.a and SBP2_9.a and the complex SBP12_9.a resulting from their interaction (cyan, orange and black, respectively) at 20 °C. c CD signal at 222 nm of the proteins SBP1_9.a and SBP2_9.a and the complex SBP12_9.a (cyan, orange and black, respectively) during thermal denaturation, the melting temperatures (T_m) are indicated in the panel. d SEC-MALS chromatograms and molecular masses for the proteins SBP1_9.a and SBP2_9.a and the complex SBP12_9.a. Theoretical Mw(SBP1_9.a) = 41.8 kDa and Mw(SBP2_9.a) = 41.7 kDa. UV signal is reported in relative absorbance units (RAU). e SAXS similarity matrix for BIP18SN, the complex SBP12_9.a and the complex SBP12_9.b. The similarity of conformations based on SASX results evaluated using the volatility ratio (V_r) metric. f Comparison of the experimental SAXS profile of the complex SBP12_9.a (black trace) with the theoretical scattering profile calculated for the BIP18SN model structure (dotted red trace) showing the difference from the single-chain protein BIP18SN. Error bars in grey represent the standard deviation for each data point in black (mean). g Topological schemes of SBP1_9.b and SBP2_9.b. CC pairs are represented as coloured helices. h CD spectra of the proteins SBP1_9.b and SBP2_9.b and the complex SBP12_9.b (cyan, orange and black, respectively) at 20 °C. i CD signal at 222 nm of the proteins SBP1_9.b and SBP2_9.b and the complex SBP12_9.b (cyan, orange and black, respectively) during thermal denaturation, the melting temperatures (T_m) are indicated in the panel. j SEC-MALS chromatograms and molecular masses for the proteins SBP1_9.b and SBP2_9.b and the complex SBP12_9.b. Theoretical Mw(SBP1_9.b) = 40.0 kDa, Mw(SBP2_9.b) = 39.7 kDa. UV signal is reported in relative absorbance units (RAU). k SAXS ab initio reconstruction superimposed on the molecular model of the SBP12_9.b complex displaying the best fit to the experimental data. l Experimental SAXS profile of the complex SBP12_9.b (black trace) matched well with the theoretical SAXS profile calculated for SBP12_9.b model structure (χ = 1.4) (orange trace). Error bars in grey represent the standard deviation for each data point in black (mean). Source data are provided as a Source Data file.