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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >Characterizing osmolyte chemical class hierarchies and functional group requirements for thermal stabilization of proteins
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Characterizing osmolyte chemical class hierarchies and functional group requirements for thermal stabilization of proteins

机译：表征渗透性化学类别层次结构和蛋白质热稳定的功能群要求

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摘要

Osmolytes are naturally occurring organic compounds that protect cellular proteins and other macromolecules against various forms of stress including temperature extremes. While biological studies have correlated the accumulation of certain classes of osmolytes with specific forms of stress, including thermal stress, it remains unclear whether or not these observations reflect an intrinsic chemical class hierarchy amongst the osmolytes with respect to effects on protein stability. In addition, very little is known in regards to the molecular elements of the osmolytes themselves that are essential for their functions. In this study, we use differential scanning fluorimetry to quantify the thermal stabilizing effects of members from each of the three main classes of protecting osmolytes on two model protein systems, C-reactive protein and tumor necrosis factor alpha. Our data reveals the absence of a strict chemical class hierarchy amongst the osmolytes with respect to protein thermal stabilization, and indicates differential responses of these proteins to certain osmolytes. In the second part of this investigation we dissected the molecular elements of amino acid osmolytes required for thermal stabilization of myoglobin and C-reactive protein. We show that the complete amino acid zwitterion is required for thermal stabilization of myoglobin, whereas removal of the osmolyte amino group does not diminish stabilizing effects on C-reactive protein. These disparate responses of proteins to osmolytes and other small molecules are consistent with previous observations that osmolyte effects on protein stability are protein-specific. Moreover, the data reported in this study support the view that osmolyte effects cannot be fully explained by considering only the solvent accessibility of the polypeptide backbone in the native and denatured states, and corroborate the need for more complex models that take into account the entire protein fabric.
机译：渗透性是天然存在的有机化合物，其保护细胞蛋白和其他大分子抵抗各种形式的应力，包括极端温度。虽然生物学研究具有与特定形式的应激形式的某些类渗透剂的积累相关，但包括热应力，仍然尚不清楚这些观察结果是否反映了渗透物中的内在化学类等级，相对于蛋白质稳定性的影响。此外，关于渗透物质的分子元素对其功能至关重要，很少少于少见。在这项研究中，我们使用差分扫描荧光测量法，以量化来自两个模型蛋白质系统，C反应蛋白和肿瘤坏死因子α的保护渗透物的每个三种主要类别中的成员的热稳定效应。我们的数据揭示了蛋白质热稳定的渗透物中没有严格的化学类层次结构，并表明这些蛋白质对某些渗透物的差异反应。在该研究的第二部分中，我们解释了肌红蛋白和C反应蛋白的热稳定所需的氨基酸渗透物的分子元素。我们表明，完全氨基酸两性期需要肌球蛋白的热稳定，而除去渗透氨基氨基的去除不会降低对C反应蛋白的稳定作用。这些不同的蛋白质对渗透蛋白和其他小分子的反应与先前的观察结果一致，即渗透物对蛋白质稳定性的影响是特异性的。此外，本研究报告的数据支持观察结果，通过考虑天然和变性状态中多肽骨架的溶剂可访问性，并证实需要更复杂的模型考虑整个蛋白质的需要完全解释渗透性效应织物。

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