The Structure of a Designed Diiron(III) Protein: Implications for Cofactor Stabilization and Catalysis

II. Electrostatic effect in the aggregat

II. Electrostatic effect in the aggregation of heat-denatured RNase A and implications for protein additive design

✍ Amos M. Tsai; John H. van Zanten; Michael J. Betenbaugh 📂 Article 📅 1998 🏛 John Wiley and Sons 🌐 English ⚖ 79 KB

In the previous study (part I), heat-denatured RNase A aggregation was shown to depend on the solution pH. Interestingly, at pH 3.0, the protein did not aggregate even when exposed to 75°C for 24 h. In this study, electrostatic repulsion was shown to be responsible for the absence of aggregates at t