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. 2017 Aug 11;7:7954. doi: 10.1038/s41598-017-08402-2

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© The Author(s) 2017

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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The cysteine pK _a in π-clamp mutants are reduced. Absorbance at 240 nm across different pHs were measured to determine the cysteine pK _a in peptide 3 (a), 1D (b) and 1E (c). (d) Rate constants for the reaction between 1 F and 2 were measured at different pHs to determine cysteine pK _a in peptide 1 F. (e) Summary of pK _a and the reaction rates of π-clamp mutants.