THERMAL-STABILITY AND PROTEIN-STRUCTURE
THERMAL-STABILITY AND PROTEIN-STRUCTURE
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DOI：
10.1021/bi00592a028
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发表时间：
1979-01-01
期刊：
影响因子：
2.9
通讯作者：
TRATSCHIN, JD
中科院分区：
文献类型：
--
作者：
ARGOS, P;ROSSMANN, MG;TRATSCHIN, JD
比较了[细菌]铁氧还蛋白、甘油醛-3-磷酸脱氢酶[来自细菌、酵母、猪和龙虾]和乳酸脱氢酶[来自细菌、鸡、猪和角鲨]的嗜热和嗜温分子的氨基酸序列。嗜温菌中的Gly、Ser、Ser、Lys和Asp通常分别被嗜热菌中的Ala、Ala、Thr、Arg和Glu取代。这些交换表明，热稳定性可以通过在整个分子中添加许多小的变化来实现，而骨架构象没有显著变化。它们的总体作用主要是增加内部疏水性和降低外部疏水性，以及有利于螺旋中的螺旋稳定残基。这些替代最大限度地减少了功能或内部残留物包装安排的中断。虽然分析仅限于上述分子，但观察到的稳定原理可能更普遍适用。
Amino acid sequences were compared for thermophilic and mesophilic molecules of [bacterial] ferredoxin, glyceraldehyde-3-phosphate dehydrogenase [from bacteria, yeast, pig and lobster] and lactate dehydrogenase [from bacteria, chicken, pig and dogfish]. Gly, Ser, Ser, Lys and Asp in mesophiles are generally substituted by Ala, Ala, Thr, Arg and Glu, respectively, in thermophiles. These exchanges suggest that thermal stability can be achieved by the addition of many small changes throughout the molecule without significant change in the backbone conformation. Their overall effect is primarily to increase internal and decrease external hydrophobicity as well as to favor helix stabilizing residues in helices. These substitutions minimize interruption of function or internal residue packing arrangements. Although the analysis was confined to the above-mentioned molecules, the observed stabilizing principles may be more generally applicable.