标题: 探讨核磁共振技术所解出的蛋白质结构其堆叠程度和演化之关系
On the Study of the Packing-Evolution Relationship in NMR Protein Structures
作者: 连冠棻
Lien, Kuan-Fen
黄镇刚
Hwang, Jenn-Kang
生物资讯及系统生物研究所
关键字: 核磁共振;蛋白质结构;序列保留;加权原子接触数目;演化;NMR;protein structure;sequence conservation;weighted contact number;evolution
公开日期: 2015
摘要: 核磁共振是用来解蛋白质三维结构的主要实验方法之一。该技术通常用于解析较小的蛋白质。在先前的结果,我们已由结晶所解出的蛋白质中,观察到结构堆叠程度和序列的保留程度存有一定相关性。藉由考虑或忽略复合体中其它的subunits,我们发现该蛋白质的结构堆叠程度会相近于它的胺基酸的保留程度。这结果显示,蛋白质可能会倾向形成有或无其他分子伴随的构形,进而在演化过程施加约束力。 在此篇研究,由核磁共振技术解出的蛋白质所组成的资料集中,藉由比较结构堆叠程度和序列的保留程度,我们发现与先前研究一致的结果。基于蛋白质的大小,我们观察到结构属性的一些明显趋势,可能在后续研究核磁共振所解出的蛋白质其结构堆叠程度时,能作为有用的指引。虽然核磁共振所解出的蛋白质结构,在过去常被认为大部分品质低落于结晶蛋白。但在我们的结果中,两者结构差异性似乎并不显着。本篇论文也许对研究核磁共振解出的蛋白质,其结构和演化间的关系有所帮助。
Nuclear Magnetic Resonance (NMR) is one of primary experimental methods to determine protein three-dimensional structures. This technique is usually used for smaller protein. In our previous study, we have observed that the structural packing profile has correlated to the sequence conservation profile of a protein determined by X-ray. By considering or ignoring other subunits in a complex, we found that the degree of structural packing of a protein will become closer to its conservation of residues. The result suggests that a protein may tend to form the conformation, which exerts constraints on its evolutionary processes, by accompanied with or without other molecules. Here, we find the consistent result that conforms our previous study in a dataset composed of NMR proteins. Based on protein size, we observe some obvious tendencies of structural properties that may be a useful guide for studying the structural packing of NMR proteins. Although NMR structures were viewed as being of generally lower quality than X-ray structures, in our result, the consequences show a small difference between the two kinds of structures. Our research may contribute to people who want to study the relationship between structure and evolution of NMR proteins.
URI: http://140.113.39.130/cdrfb3/record/nctu/#GT070057214
http://hdl.handle.net/11536/126759
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