摘要
单一氨基酸的置换可以改变酶的热稳定性。脯氨酸 (Pro)残基在蛋白质结构及其热稳定性中具有特殊作用。它十分偏爱 β 转折或无规卷曲结构 ,而很少出现在α 螺旋和 β 折叠中。分析认为在改善酶热稳定性的蛋白质工程中 ,只要主链构象不发生骤变 ,则可在适当的β 转折或无规卷曲中引入Pro ,通过其刚性的吡咯烷环 ,降低蛋白质去折叠时的骨架熵 ,从而使其周围的构象更合理。这一Pro理论 (theprolinetheory)的分子设计新思路将会得到进一步的发展和完善。
Thermostability of enzymes can be altered by single amino acid substitution. Prolines play very specific roles in protein secondary structure and heat stability. They prefer β\|turns and random coils, but are rarely found in α\|helices and β\|sheets. Improvement in thermostability of enzymes by protein engineering may introduce Pro at suitable β\|turns and random coils. The rigid pyrrolidine ring can make the conformation of surroundings to be more reasonable by reducing the backbone unfolding entropy of proteins. This new prolines theory will be improved and become perfect.
出处
《生物工程进展》
CSCD
2000年第4期48-51,共4页
Progress in Biotechnology
关键词
脯氨酸
二级结构
热稳定性
蛋白质工程
Proline, Secondary structure, Thermostability, Protein engineering
