Comparison of the dynamic structure of α-chymotrypsin in aqueous solution and in reversed micelles by fluorescent active-site probing

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