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Structure and Properties of Native and Unfolded Lysing Enzyme From T. Harzianum: Chemical and pH Denaturation

Structure and Properties of Native and Unfolded Lysing Enzyme From T. Harzianum: Chemical and pH Denaturation

Houda Bey, Wala Gtari, Adel Aschi, Tahar Othman

Int J Biol Macromol. 2016 Nov;92:860-866.

PMID: 27496603

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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR424807	Lysing Enzymes from Trichoderma harzianum			Price

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