Thermostability of Salt Bridges versus Hydrophobic Interactions in Proteins Probed by Statistical Potentials

Stability and activity modulation of chy

Stability and activity modulation of chymotrypsins in AOT reversed micelles by protein–interface interaction: Interaction of α-chymotrypsin with a negative interface leads to a cooperative breakage of a salt bridge that keeps the catalytic active conformation (Ile16–Asp194)

✍ Fábio C. L. Almeida; Ana Paula Valente; Hernan Chaimovich 📂 Article 📅 1998 🏛 John Wiley and Sons 🌐 English ⚖ 76 KB 👁 2 views

The stability of ␣-chymotrypsin and ␦-chymotrypsin was studied in reversed micelles of sodium bis(2ethylhexyl)sulfosuccinate (AOT) in isooctane. ␣-Chymotrypsin is inactivated at the interface and at the water pool, while ␦-chymotrypsin is inactivated only at the water pool. The mechanism of inactiva