Thermodynamic evaluation and modeling of proton and water exchange associated with benzamidine and berenil binding to ß-trypsin

Author:

Pereira M.T.1,Silva-Alves J.M.2,Martins-José A.3,Lopes J.C.D.3,Santoro M.M.2

Affiliation:

1. Universidade Federal de Minas Gerais; Universidade Federal de Minas Gerais

2. Universidade Federal de Minas Gerais

3. Universidade Federal de Minas Gerais, Brasil

Publisher

FapUNIFESP (SciELO)

Subject

Cell Biology,General Pharmacology, Toxicology and Pharmaceutics,General Medicine,Immunology,Physiology,Biochemistry,General Neuroscience,Biophysics

Reference39 articles.

1. Structural and energetic determinants of the S1-site specificity in serine proteases;Czapinska H;European Journal of Biochemistry,1999

2. Different binding orientations for the same agonist at homologous receptors: a lock and key or a simple wedge?;Mu T;Journal of the American Chemical Association,2003

3. Electrostatic lock-and-key model for the study of biological isosterism: role of structural water in the binding of basic pancreatic trypsin inhibitor to beta-trypsin;Naray-Szabo G;Enzyme,1986

4. Membrane anchored serine-proteases: a rapidly expanding group of cell surface proteolytic enzymes with potential roles in cancer;Netzel-Arnett S;Cancer and Metastasis Reviews,2003

5. Conservation of digestive enzymes;Rothman S;Physiological Reviews,2002

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