Structure-dependent relationships between growth temperature of prokaryotes and the amino acid frequency in their proteins
Structure-dependent relationships between growth temperature of prokaryotes and the amino acid frequency in their proteins
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DOI：
10.1007/s00792-007-0072-3
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发表时间：
2007-07-01
期刊：
影响因子：
2.9
通讯作者：
Jonassen, Inge
中科院分区：
文献类型：
--
作者：
Saelensminde, Gisle;Halskau, Oyvind, Jr.;Jonassen, Inge
我们研究了适应0-102摄氏度温度的原核物种同源物之间的氨基酸频率和取代模式，发现许多氨基酸的频率存在显著的温度依赖性差异。当我们分别分析表面和核心残留物时，这一点特别明显。表面和核心之间的差异在适应温暖环境的蛋白质中变得更加明显，具有更疏水的核心，以及蛋白质表面上更多的带电和长链氨基酸。我们还发现，嗜温生物的氨基酸组成与嗜冷生物比嗜热生物更相似，而古生菌的替换模式似乎与细菌略有不同。
We studied the amino acid frequency and substitution patterns between homologues of prokaryotic species adapted to temperatures in the range 0-102 degrees C, and found a significant temperature-dependent difference in frequency for many of the amino acids. This was particularly clear when we analysed the surface and core residues separately. The difference between the surface and the core is getting more pronounced in proteins adapted to warmer environments, with a more hydrophobic core, and more charged and long-chained amino acids on the surface of the proteins. We also see that mesophiles have a more similar amino acid composition to psychrophiles than to thermophiles, and that archea appears to have a slightly different pattern of substitutions than bacteria.