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. 2017 Jul 18;45(16):9760–9772. doi: 10.1093/nar/gkx609

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© The Author(s) 2017. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

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Figure 4. — The SnoaL_2 domain contributes to a compact σ^J conformation. (A) Comparison of analytical size exclusion chromatogram of σ^J and σ^JΔSnoaL_2. The apparent molar mass (28.5 kDa) of the σ^JΔSnoaL_2 protein is higher than expected (19.1 kDa) for a monomer. (B) Molecular dynamics (MD) simulations provide a basis for a comparison between the conformations sampled by σ^J and σ^JΔSnoaL_2. The considerable conformational heterogeneity noted in the MD simulations for σ^JΔSnoaL_2 is consistent with the hypothesis that the SnoaL_2 domain constraints σ^J to a compact structure. (C) A comparison between the proteolytic susceptibility of σ^J and σ^JΔSnoaL_2 (using trypsin) revealed that σ^JΔSnoaL_2 is significantly more proteolytically labile when compared to full length σ^J.