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. Author manuscript; available in PMC: 2019 Jul 25.
Published in final edited form as: J Am Chem Soc. 2018 Jul 16;140(29):9108–9119. doi: 10.1021/jacs.8b02129

Figure 4.

Figure 4.

(A) Graphical illustration of the entropy terms associated with Zn binding to the wild- type vs CzrA variants derived from calorimetric (total, eq 1; resulting for binding two Zn equivalent per dimer) and internal protein dynamics measurements (ΔSaxis2, Conf, eq 7) by NMR spectroscopy. The vertical scale bar corresponds to a change of 2.0 kcal mol−1. The variants marked in bold show conformational exchange in the Zn-bound state. (B) Site-specific methyl Rex in the apo- and Zn2-loaded in L34A CzrA homodimers mapped onto the structure of apo- and Zn2-loaded, respectively.