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Increasing protein conformational stability by optimizing beta-turn sequence

机译：通过优化β-转角序列提高蛋白质构象稳定性

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摘要

Protein conformational stability is an important concern in many fields. Here, we describe a strategy for significantly increasing conformational stability by optimizing beta-turn sequence. Proline and glycine residues are statistically preferred at several beta-turn positions, presumably because their unique side-chains contribute favorably to conformational stability in certain P-turn positions. However, beta-turn sequences often deviate from preferred proline or preferred glycine. Therefore, our strategy involves replacing non-proline and non-glycine beta-turn residues with preferred proline or preferred glycine residues. Here, we develop guidelines for selecting appropriate mutations, and present results for five mutations (S31P, S42G, S48P, T76P, and Q77G) that significantly increase the conformational stability of RNase Sa. The increases in stability ranged from 0.7 kcal/mol to 1.3 kcal/mol. The strategy was successful in overlapping or isolated beta-turns, at buried (up to 50%) or completely exposed sites, and at relatively flexible or inflexible sites. Considering the significant number of U-turn residues in every globular protein and the frequent deviation of U-turn sequences from preferred proline and preferred glycine residues, this simple, efficient strategy will be useful for increasing the conformational stability of proteins. (C) 2007 Elsevier Ltd. All rights reserved.
机译：蛋白质构象稳定性是许多领域中的重要问题。在这里，我们描述了一种通过优化β-turn序列显着增加构象稳定性的策略。统计学上优选脯氨酸和甘氨酸残基在几个β-转角位置，因为它们的独特侧链有利于在某些P-转角位置的构象稳定性。然而，β-转角序列常常偏离优选的脯氨酸或优选的甘氨酸。因此，我们的策略涉及用优选的脯氨酸或优选的甘氨酸残基取代非脯氨酸和非甘氨酸的β-turn残基。在这里，我们制定了选择合适突变的指南，并给出了五个突变（S31P，S42G，S48P，T76P和Q77G）的结果，这些突变显着增加了RNase Sa的构象稳定性。稳定性的增加范围为0.7kcal / mol至1.3kcal / mol。该策略在重叠的或孤立的β形转弯，埋入的（高达50％）或完全暴露的位置以及相对灵活或不灵活的位置上都成功。考虑到每个球状蛋白中大量的U形转残基以及U形转弯序列与首选脯氨酸和首选甘氨酸残基的频繁偏离，这种简单，有效的策略对于增加蛋白质的构象稳定性将是有用的。 （C）2007 Elsevier Ltd.保留所有权利。

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