Fig. 1 | Nature Communications

Fig. 1

From: A binding cooperativity switch driven by synergistic structural swelling of an osmo-regulatory protein pair

Fig. 1

Breakdown of structure-stability relationship. a The structure of Cnu indicating the four helices and aromatic residues. b Electrostatic potential map of Cnu highlighting the large asymmetry in charge distribution. c, d Absolute heat capacity profiles (c) and the far-UV CD monitored thermal unfolding curves (d) at the representative ionic strength conditions. e The degree of secondary structure (ordinate) as a function of ionic strength at 25 °C (abscissa). The three representative conditions are marked in blue (14.5 mM), green (170 mM), and red (500 mM), respectively. Additional spectra were acquired at various intermediate ionic strengths spanning the representative conditions (open circles). f Near-UV CD spectra at 5 °C display significant tertiary structural differences at low ionic strength (<100 mM) compared to high IS conditions. Source data are provided as a Source Data file

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