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 co...

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Bibliographic Details
Published in:Brazilian journal of physics 2017-10, Vol.47 (5), p.524-531
Main Authors: Perez, Aline Sanches, Oliveira, Cristiano Luis Pinto
Format: Article
Language:English
Subjects:
Agglomeration
Denaturation
Dichroism
Fluorescence
General and Applied Physics
Heat measurement
Lysozyme
Physics
Physics and Astronomy
Proteins
Serum albumin
Thermodynamic equilibrium
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Summary: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.
ISSN:0103-9733
1678-4448
DOI:10.1007/s13538-017-0520-1