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. 2023 Nov 1;32(11):e4769. doi: 10.1002/pro.4769

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© 2023 The Authors. Protein Science published by Wiley Periodicals LLC on behalf of The Protein Society.

This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc-nd/4.0/ License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non‐commercial and no modifications or adaptations are made.

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Experimental characterization of designed proteins. (a) Model of the four designs 513, 515, 518, and 540 with zoom in views showing the indicated (*) pH‐responsive hydrogen bond network. Black lines represent hydrogen bond network layers. The C‐terminal helix (yellow) carries phenylalanines for membrane disruption (red). Size exclusion chromatography chromatogram (A280 = absorbance at 280 nm, AU = arbitrary units) (b), circular dichroism (CD) spectra (c), and dynamic light scattering (DLS) results (d) of the four proteins are shown. CD spectra and DLS data were collected at close to neutral pH and pH 5 (see Section 4 for details).