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进化与无序。

Evolution and disorder.

机构信息

Department of Biological Sciences, IBEST, University of Idaho, Moscow, ID 83844-3051, United States.

出版信息

Curr Opin Struct Biol. 2011 Jun;21(3):441-6. doi: 10.1016/j.sbi.2011.02.005. Epub 2011 Apr 7.

DOI:10.1016/j.sbi.2011.02.005
PMID:21482101
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3112239/
Abstract

The evolution of disordered proteins or regions of proteins differs from that of ordered proteins because of the differences in their sequence composition, intramolecular contacts, and function. Recent assessments of disordered protein evolution at the sequence, structural, and functional levels support this hypothesis. Disordered proteins have a different pattern of accepted point mutations, exhibit higher rates of insertions and deletions, and generally, but not always, evolve more rapidly than ordered proteins. Even with these high rates of sequence evolution, a few examples have shown that disordered proteins maintain their flexibility under physiological conditions, and it is hypothesized that they maintain specific structural ensembles.

摘要

无序蛋白质或蛋白质区域的进化与有序蛋白质的进化不同,这是由于它们在序列组成、分子内接触和功能上的差异。最近在序列、结构和功能水平上对无序蛋白质进化的评估支持了这一假设。无序蛋白质具有不同的可接受点突变模式,表现出更高的插入和缺失率,通常但并非总是比有序蛋白质进化得更快。即使在这些高序列进化率的情况下,也有一些例子表明,无序蛋白质在生理条件下保持其灵活性,并且假设它们保持特定的结构集合。

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本文引用的文献

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Phosphorylated and nonphosphorylated serine and threonine residues evolve at different rates in mammals.磷酸化和非磷酸化的丝氨酸和苏氨酸残基在哺乳动物中以不同的速率进化。
Mol Biol Evol. 2010 Nov;27(11):2548-54. doi: 10.1093/molbev/msq142. Epub 2010 Jun 9.
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Signatures of protein biophysics in coding sequence evolution.编码序列演化中的蛋白质生物物理学特征。
Curr Opin Struct Biol. 2010 Jun;20(3):385-9. doi: 10.1016/j.sbi.2010.03.004. Epub 2010 Apr 13.
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Aquifex aeolicus FlgM protein exhibits a temperature-dependent disordered nature.嗜热栖热菌FlgM蛋白表现出温度依赖性的无序特性。
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Roles of “junk phosphorylation” in modulating biomolecular association of phosphorylated proteins?“垃圾磷酸化”在调节磷酸化蛋白质的生物分子缔合中的作用?
Cell Cycle. 2010 Apr 1;9(7):1276-80. doi: 10.4161/cc.9.7.11066.
5
Protein secondary structure appears to be robust under in silico evolution while protein disorder appears not to be.蛋白质二级结构在计算机模拟进化中似乎很稳定,而蛋白质无序结构似乎则不然。
Bioinformatics. 2010 Mar 1;26(5):625-31. doi: 10.1093/bioinformatics/btq012. Epub 2010 Jan 16.
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Solution structure of the C-terminal X domain of the measles virus phosphoprotein and interaction with the intrinsically disordered C-terminal domain of the nucleoprotein.麻疹病毒磷蛋白 C 末端 X 结构域的溶液结构及其与核蛋白固有无序 C 末端结构域的相互作用。
J Mol Recognit. 2010 Sep-Oct;23(5):435-47. doi: 10.1002/jmr.1010.
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