Thermal-Induced Denaturation and Aggregation Behavior of Lysozyme and Bovine Serum Albumin: a Thermodynamic and Structural Study


Solution studies permit a direct investigation of the particles on a well-defined environment. Fluorescence, circular dichroism, scattering, and calorimetry provide, individually, very important information among the protein structure, overall shape, and thermodynamic equilibrium. In this work, a combination of these techniques is presented for the study of denaturation induced by temperature of two well-known proteins, Henn Egg lysozyme and bovine serum albumin. A detailed thermodynamic and structural investigation is shown for these proteins, providing interesting information on the thermal-induced changes in the protein structure and aggregation behavior.

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The authors are grateful to Dra. Renata N. Bicev for the support on sample preparation and SAXS measurements, Dra. Laura Farkuh for the support on DSC measurements, Dr. Yang Sun for the support on fluorescence measurements and valuable discussions, and Dra. Valquiria P. Souza for the support on CD measurements. ASP is supported by CAPES and INCT-FCx. CLPO is supported by FAPESP, CNPQ, and INCT-FCx.

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Correspondence to Cristiano Luis Pinto Oliveira.

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Perez, A.S., Oliveira, C.L.P. Thermal-Induced Denaturation and Aggregation Behavior of Lysozyme and Bovine Serum Albumin: a Thermodynamic and Structural Study. Braz J Phys 47, 524–531 (2017).

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  • Proteins
  • Small-angle X-ray scattering
  • SAXS
  • Modeling
  • Protein structure
  • DSC