The Thermodynamics of Protein–Protein Recognition as Characterized by a Combination of Volumetric and Calorimetric Techniques: The Binding of Turkey Ovomucoid Third Domain to α-Chymotrypsin

NMR chemical shift mapping of the bindin

NMR chemical shift mapping of the binding site of a protein proteinase inhibitor: changes in the 1H, 13C and 15N NMR chemical shifts of turkey ovomucoid third domain upon binding to bovine chymotrypsin Aα

✍ Jikui Song; John L. Markley 📂 Article 📅 2001 🏛 John Wiley and Sons 🌐 English ⚖ 201 KB

## Abstract The substrate‐like inhibition of serine proteinases by avian ovomucoid domains has provided an excellent model for protein inhibitor‐proteinase interactions of the standard type. ^1^H,^15^N and ^13^C NMR studies have been undertaken on complexes formed between turkey ovomucoid third dom