Calorimetric study of the thermal unfolding of Kunitz-type soybean trypsin inhibitor at pH 7.0
Author:
Publisher
Elsevier BV
Subject
Physical and Theoretical Chemistry,Condensed Matter Physics,Instrumentation
Reference29 articles.
1. CRYSTALLINE SOYBEAN TRYPSIN INHIBITOR
2. Comparative Study on Amino Acid Sequences of Kunitz-Type Soybean Trypsin Inhibitors, Tia, Tib, and Tic1
3. Crystal structure of the complex of porcine trypsin with soybean trypsin inhibitor (Kunitz) at 2.6 Å resolution
4. Heat of reaction between trypsin and soybean trypsin inhibitor
5. Reaction heat variation with pH in formation of the trypsin-soybean inhibitor complex.
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1. Tentative Assignment of the Potato Serine Protease Inhibitor Group as β-II Proteins Based on Their Spectroscopic Characteristics;Journal of Agricultural and Food Chemistry;2004-11-10
2. Experiment-guided thermodynamic simulations on reversible two-state proteins: implications for protein thermostability;Biophysical Chemistry;2004-11
3. Temperature Range of Thermodynamic Stability for the Native State of Reversible Two-State Proteins;Biochemistry;2003-04-11
4. Reversible denaturation of the soybean Kunitz trypsin inhibitor;Archives of Biochemistry and Biophysics;2003-04
5. Maximal Stabilities of Reversible Two-State Proteins;Biochemistry;2002-04-01
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