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

May 22, 2018

Title

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

Author

Aline Sanches Perez, Cristiano Luis Pinto Oliveira

Year

2017

Journal

Brazilian Journal of Physics

Abstract

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.

Instrument

J-715

Keywords

Circular dichroism, Secondary structure, Thermal stability, Biochemistry