Structure and properties of native and unfolded lysing enzyme from T. harzianum: Chemical and pH denaturation

被引：7
|
作者：
Bey, Houda [1 ]
Gtari, Wala [1 ]
Aschi, Adel [1 ]
Othman, Tahar [1 ]
机构：
[1] Univ Tunis El Manor, Fac Sci Tunis, Lab Phys Mat Molle & Modelisat Electromagnet LR99, Tunis 2092, Tunisia
来源：
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES | 2016年 / 92卷
关键词：
Lysing enzyme from T. harzianum; Dynamic light scattering; Turbidimetry; Unfolded proteins; Compaction; Dynamic molecular analysis; GUANIDINE-HYDROCHLORIDE DENATURATION; 3-DIMENSIONAL FOURIER SYNTHESIS; ALPHA-CHYMOTRYPSIN; PROTEIN-STRUCTURE; CELL-WALL; AGGREGATION; UREA; ELECTROSTATICS; RIBONUCLEASE; COMPACTION;
D O I：
10.1016/j.ijbiomac.2016.08.001
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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. (C) 2016 Elsevier B.V. All rights reserved.
引用
收藏
页码：860 / 866
页数：7
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