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. 2019 Sep 4;10:3984. doi: 10.1038/s41467-019-11930-2

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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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Fig. 2 — Selective allosteric effects initiated by cAMP binding. Force-extension curves (a, d), unfolding force probability distributions (b, e), and force-dependent folded-state lifetimes (c, f) for the CNB-B (top) and CNB-A (bottom) domains. Numbering corresponds to the isolated CNB domains in the apo (1) or cAMP-bound states (2), and selective unfolding of the CNB domains bound to cAMP (3). The red arrow in d indicates the unfolding of the N3A motif. Source data for a through d are provided as a Source Data file. g Structural alignment of the CNB-A (light purple) and CNB-B (dark blue) domains bound to cAMP (red). h Energy landscape and free energy of the CNB domains due to cAMP binding and inter-domain contacts. The height of the energy barriers reflects the folded and unfolded-state lifetimes of the CNB domains in the different states. The energy landscapes have been normalized to the unfolded state. (Supplementary Tables 1 and 2)