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• W1977640049 startingPage "11435" @default.
• W1977640049 abstract "In an effort to relate structural, kinetic, and thermodynamic features in a model macromolecular recognition process, the amino acid residues in the reactive surface of bovine pancreatic trypsin inhibitor (BPTI) and surrounding residues were substituted individually by alanine, and the effects of the point-mutations on the kinetics and thermodynamics of inhibition by BPTI toward trypsin and chymotrypsin were investigated. Fifteen alanine mutants were produced. The majority of the BPTI mutants exhibited a binding affinity similar to that of the wild-type protein. The exceptions were the primary specificity site (P1) mutant and those mutants that seem to have nonlocal perturbations of structure, as revealed by circular dichroism and thermostability measurements. The mutation at the P1 site caused a reduction in the binding free energy of 10 and 1.8 kcal mol-1 for trypsin and chymotrypsin, respectively. The losses in binding affinity were determined almost exclusively by an increase in the dissociation rate constant. However, the rate of association of the P1 mutant, Lys-15-Ala, with trypsin was also drastically reduced (>200-fold). Calorimetric measurements of the heats of binding for the association of chymotrypsin with the wild-type inhibitor and its alanine mutants allowed determination of the relative contributions of the changes in enthalpy and entropy to the free energy of binding. Compensatory changes in the two parameters were observed in several cases, which were attributed to desolvation effects at the binding interface." @default.
• W1977640049 created "2016-06-24" @default.
• W1977640049 creator A5037578536 @default.
• W1977640049 creator A5083934494 @default.
• W1977640049 date "1996-01-01" @default.
• W1977640049 modified "2023-09-27" @default.
• W1977640049 title "Alanine Point-Mutations in the Reactive Region of Bovine Pancreatic Trypsin Inhibitor: Effects on the Kinetics and Thermodynamics of Binding to β-Trypsin and α-Chymotrypsin" @default.
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• W1977640049 doi "https://doi.org/10.1021/bi960515w" @default.
• W1977640049 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8784199" @default.
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