Jia Mengwen, Luo Liaofu
Laboratory of Theoretical Biophysics, Faculty of Science and Technology, Inner Mongolia University, Hohhot 010021, China.
Biochem Biophys Res Commun. 2006 Apr 28;343(1):177-82. doi: 10.1016/j.bbrc.2006.02.135. Epub 2006 Mar 3.
About 200 mRNA sequences of Escherichia coli and human with matching protein secondary structure data were studied. The mRNA folding for each native sequence and for corresponding randomized sequences was calculated through free energy minimization. We have found that the folding energy of mRNA segments in different protein secondary structures is significantly different. The average Z score is more negative for regular secondary structure (alpha-helix and beta-strand) than that for coil. This suggests that the codon choice in native mRNA sequence coding for protein regular structure contributes more to the mRNA folding stability.
研究了约200个具有匹配蛋白质二级结构数据的大肠杆菌和人类的mRNA序列。通过自由能最小化计算每个天然序列及其相应随机序列的mRNA折叠情况。我们发现，不同蛋白质二级结构中mRNA片段的折叠能量存在显著差异。规则二级结构（α-螺旋和β-链）的平均Z分数比卷曲结构的更负。这表明，编码蛋白质规则结构的天然mRNA序列中的密码子选择对mRNA折叠稳定性的贡献更大。
