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首页> 外文期刊>Biochemistry >Structure of beta-Purothionin in Membranes:A Two-Dimensional Infrared Correlation Spectroscopy Study
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Structure of beta-Purothionin in Membranes:A Two-Dimensional Infrared Correlation Spectroscopy Study

机译：β-Purothionin在膜中的结构：二维红外相关光谱研究。

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Two-dimensional infrared correlation spectroscopy has been used to investigate the structure of beta-purothionin,a small basic protein found in the endosperm of wheat seeds,in the absence and presence of dimyristoylphosphatidylglycerol (DMPG) membranes.To generate the two-dimensional synchronous and asynchronous maps,hydrogen-deuterium exchange of the protein amide protons has been used as an external perturbation.This method has allowed us to separate the different secondary structure elements and side chain contributions in the regions of amide I,II,and II' bands to determine that the relative order of deuteration of the beta-purothionin protons is as follows:turns,asparagines,and lysines > unordered structure and tyrosine > beta-sheet > a-helices and arginines.The results also indicate that the protein undergoes significant changes both in secondary structure and in deuteration in the presence of DMPG bilayers.The helical content of beta-purothionin is higher in the presence of the lipid,and the relative order of deuteration is as follows:lysines and arginines > asparagines and beta-sheet > unordered structure and a-helices.The inversion in the deuteration order of the arginine residues is assigned to a change of the degree of association of the protein in the membrane.In addition,the results reveal that the part of the protein containing the tyrosine residue interacts with the lipid membrane.Our results combined with those previously published suggest that the toxicity of beta-purothionin is more associated with the formation of functional channels in cell membranes rather than with a lytic phenomenon.
机译：二维红外相关光谱法已被用于研究β-嘌呤硫醚的结构，该蛋白是在小麦种子的胚乳中发现的一种小的碱性蛋白，在没有二甲基香豆素基磷脂酰甘油（DMPG）膜的情况下存在。异步图谱，蛋白质酰胺质子的氢-氘交换已被用作外部扰动。这种方法使我们能够分离出不同的二级结构元素和酰胺I，II和II'区域中的侧链贡献。确定β-硫氧磷蛋白质子的氘代相对顺序如下：弯头，天冬酰胺和赖氨酸>无序结构和酪氨酸>β-折叠> a-螺旋和精氨酸。结果还表明该蛋白都经历了显着变化在存在DMPG双层的情况下，处于二级结构和氘化状态。脂质和氘化的相对顺序如下：赖氨酸和精氨酸>天冬酰胺和β-折叠>无序结构和a螺旋。精氨酸残基的氘化顺序颠倒被赋予了缔合度的变化此外，结果表明，含有酪氨酸残基的蛋白质部分与脂质膜相互作用。我们的结果与先前发表的结果相结合，表明β-硫氧磷蛋白的毒性与环糊精的形成有关。细胞膜中的功能性通道而不是溶解现象。

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