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首页> 外文期刊>RSC Advances >Metal ions provide structural stability and compactness to tetrameric purothionin
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Metal ions provide structural stability and compactness to tetrameric purothionin

机译：金属离子为四聚硫氧磷蛋白提供结构稳定性和致密性

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摘要

Antimicrobial plant protein purothionin plays a significant role in immunity and microbial defense systems in plants and animals. From the molecular simulation analyses and spectroscopic investigation, it was observed that the structural arrangement of the protein tetramer attained much more stable and compact conformation in the presence of calcium and magnesium compared to the tetramer alone in the absence of ions. An increase in the folded secondary structure in the presence of calcium and magnesium ions was observed. The circular dichroism spectral analysis and FT-IR study along with molecular dynamics simulation studies suggested some increase in the helical content/compactness of the protein. Structural stability of the protein, as observed, may be linked to increased antifungal activity against pathogens like Candida albicans, Candida krusei and Candida parapsilosis.
机译：抗菌植物蛋白Purothionin在动植物的免疫和微生物防御系统中起着重要作用。从分子模拟分析和光谱学研究中，观察到与不存在离子的情况下单独的四聚体相比，存在钙和镁的情况下蛋白质四聚体的结构排列获得了更加稳定和紧凑的构象。观察到在钙和镁离子存在下折叠二级结构的增加。圆二色谱光谱分析和FT-IR研究以及分子动力学模拟研究表明，该蛋白质的螺旋含量/致密性有所提高。如所观察到的，该蛋白质的结构稳定性可能与对病原体例如白色念珠菌，克鲁斯念珠菌和副念珠菌的抗真菌活性增加有关。

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