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天然蛋白质与通过反转氨基酸序列获得的嵌合体构建体之间的结构相似性。

Structural similarity between native proteins and chimera constructs obtained by inverting the amino Acid sequence.

作者信息

Carugo Oliviero

出版信息

Acta Chim Slov. 2010 Dec;57(4):936-40.

PMID:24061900
Abstract

The analysis of the symmetry of protein three-dimensional structures can be extremely useful in order to understand and classify the protein structural universe. The structures of proteins with back-traced amino acid sequence were modeled and compared to the structures of their native counterparts. Only in a very limited set of cases, the two objects showed a significant level of similarity. These extremely symmetric examples can be of any structural class and of any dimension. The lack of biunique "N to C" and "C to N" symmetry at the structural level mirrors that at the sequence level and we propose to design as a dlof symmetry the cases in which a protein structure is similar to its back-traced variant.

摘要

对蛋白质三维结构的对称性进行分析,对于理解和分类蛋白质结构体系极为有用。对具有反向追踪氨基酸序列的蛋白质结构进行建模,并与它们天然对应物的结构进行比较。只有在非常有限的一组情况下,这两个对象才显示出显著程度的相似性。这些极其对称的例子可以属于任何结构类别和任何维度。在结构层面上缺乏“从N到C”和“从C到N”的唯一对称性,反映了序列层面上的情况,我们建议将蛋白质结构与其反向追踪变体相似的情况设计为一种对称性缺失(dlof symmetry)。

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Structural similarity between native proteins and chimera constructs obtained by inverting the amino Acid sequence.天然蛋白质与通过反转氨基酸序列获得的嵌合体构建体之间的结构相似性。
Acta Chim Slov. 2010 Dec;57(4):936-40.
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