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Published on: March 25, 2017
Structure and properties of native and unfolded lysing enzyme from T. harzianum: Chemical and pH denaturation
Houda Bey1, Wala Gtari1, Adel Aschi1
1Université de Tunis El Manar, Faculté des Sciences de Tunis, LR99ES16 Laboratoire Physique de la Matière Molle et de la Modélisation Électromagnétique, 2092, Tunis, Tunisie.
Abstract:
The effect of chemical denaturants and pH on the change of the conformation of the protein Lysing Enzyme from Trichoderma Harzianum has been investigated by dynamic light scattering (DLS) and turbidimetry. Chemical denaturants are frequently used to describe the mechanisms of folding and transition states. We have analyzed the pH effect on the properties and particle size of the protein. The compaction factor CI has shown that the protein is weakly disordered. The molecular dynamics simulations confirm, at neutral pH, that the protein has a low net charge and high hydrophobicity.
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