Thermodynamic Analysis of the Conformational Stability of a Single-Domain Therapeutic Antibody
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The stability of a new single-domain therapeutic antibody to the ErbB3 receptor was studied by fluorescence spectroscopy at different concentrations of a denaturing agent and temperatures. The analysis of experimental denaturation curves allowed us to build a complete thermodynamic model of unfolding and to determine all parameters of the transition: ΔG = 8.5 kcal mol–1, T m = 76°C, ΔH m = 107 kcal mol–1, ΔC p = 1.8 kcal K–1 mol–1. The obtained data evidence the high stability of the antibody in a broad range of conditions, which is essential for further structural and functional studies and possible therapeutic application.
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