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首页> 外文期刊>Journal of Molecular Structure >Conformational assignment of the N-terminal residues of the small domain(A1a 12-Val 49)of pig cytosolic aspartate aminotransferase using the ACAP computer program
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Conformational assignment of the N-terminal residues of the small domain(A1a 12-Val 49)of pig cytosolic aspartate aminotransferase using the ACAP computer program

机译:使用ACAP计算机程序对猪胞质天冬氨酸转氨酶小结构域(A1a 12-Val 49)的N端残基进行构象分配

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摘要

Conformational changes of the aspartate aminotransferase N-terminal small domain residues A1a12-Va149 that occur upon substratte binding were evaluated using Amino Acid Conformation Assignment of Proteins(ACAP) computer program(Version1.07).In the segment considered,four residues(Va115,Asp27,Gly36 andGly38)underwent backbone torsional angle changes of such magnitude that led to different conformers,while the other residues underwent change in backbone torsional angles without change in their conformational assignment.The residues that changed conformational assignment migrated to adjacent conformational centers of the Ramachandran map.In addition to confirming the importance of three residues for enzyme's function (Ala12,Gly36,Gly38),the conformational analysis revealed an additional potentially significant residue(Asp27),These findings are consistent with X-ray studies and literature values for aspartate aminotransferase(AspAT),showing that the ACAP program can be successfully used in determinig conformational assignment of amino acid residues within proteins.The approach can be used to predict amino acid residue function in cases where it would be difficult to infer such information from the X-ray studies.
机译:使用氨基酸构象分配蛋白(ACAP)计算机程序(Version 1.07)评估了亚基结合后天冬氨酸转氨酶N末端小域残基A1a12-Va149的构象变化。在所考虑的片段中,共有四个残基(Va115, Asp27,Gly36和Gly38)的骨架扭转角发生了变化,从而导致不同的构象异构体,而其他残基的骨架扭转角发生了变化,而其构象分配没有变化。改变构象分配的残基迁移到了Ramachandran的相邻构象中心除了确认三个残基对酶功能的重要性(Ala12,Gly36,Gly38)外,构象分析还发现了一个潜在的重要残基(Asp27),这些发现与X射线研究和天冬氨酸转氨酶的文献价值一致(AspAT),表明ACAP程序可以成功用于确定蛋白质中氨基酸残基的构象分配。在难以从X射线研究推断此类信息的情况下,该方法可用于预测氨基酸残基的功能。

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