嗜热蛋白和嗜温蛋白的鉴别
Discrimination of thermophilic and mesophilic proteins.
作者信息
Taylor Todd J, Vaisman Iosif I
机构信息
National Cancer Institute, Laboratory of Molecular Biology, 37 Convent Dr, MS 4264, Bethesda, MD 20892, USA.
出版信息
BMC Struct Biol. 2010 May 17;10 Suppl 1(Suppl 1):S5. doi: 10.1186/1472-6807-10-S1-S5.
BACKGROUND
There is a considerable literature on the source of the thermostability of proteins from thermophilic organisms. Understanding the mechanisms for this thermostability would provide insights into proteins generally and permit the design of synthetic hyperstable biocatalysts.
RESULTS
We have systematically tested a large number of sequence and structure derived quantities for their ability to discriminate thermostable proteins from their non-thermostable orthologs using sets of mesophile-thermophile ortholog pairs. Most of the quantities tested correspond to properties previously reported to be associated with thermostability. Many of the structure related properties were derived from the Delaunay tessellation of protein structures.
CONCLUSIONS
Carefully selected sequence based indices discriminate better than purely structure based indices. Combined sequence and structure based indices improve performance somewhat further. Based on our analysis, the strongest contributors to thermostability are an increase in ion pairs on the protein surface and a more strongly hydrophobic interior.
背景
关于嗜热生物蛋白质热稳定性的来源已有大量文献。了解这种热稳定性的机制将有助于全面了解蛋白质，并有助于设计合成超稳定生物催化剂。
结果
我们使用中温-嗜热直系同源物对集，系统地测试了大量从序列和结构衍生出的量，以判断它们区分热稳定蛋白质与其非热稳定直系同源物的能力。测试的大多数量对应于先前报道的与热稳定性相关的特性。许多与结构相关的特性源自蛋白质结构的德劳内三角剖分。
结论
精心挑选的基于序列的指标比纯粹基于结构的指标具有更好的区分能力。基于序列和结构的综合指标在一定程度上进一步提高了性能。根据我们的分析，对热稳定性贡献最大的因素是蛋白质表面离子对的增加和更疏水的内部结构。
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