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首页> 外文期刊>The journal of physical chemistry, B. Condensed matter, materials, surfaces, interfaces & biophysical >Mechanical Softening of a Small Ubiquitin-Related Modifier Protein Due to Temperature Induced Flexibility at the Core
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Mechanical Softening of a Small Ubiquitin-Related Modifier Protein Due to Temperature Induced Flexibility at the Core

机译：由于温度诱导芯的柔性，小泛素相关改性剂蛋白的机械软化

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Despite the growing interest in the thermal softening of proteins, the mechanistic details of it are far from understood. beta-Grasp proteins have globular shape with compact structure and they are mechanically resilient. The beta-clamp or mechanical clamp in them formed by the interactions between the terminal beta-strands is generally associated with the protein mechanical resistance. Although previous studies showed that temperature can perturb the protein mechanical stability, the structural changes leading to the lowered mechanical resistance are not known. Here, we investigated the temperature dependent mechanical stability of small ubiquitin-related modifier 2 (SUMO2) using single-molecule force spectroscopy (SMFS) and the corresponding conformational changes using ensemble experiments. SMFS studies on the polyprotein of SUMO2 estimate a decrease in the spring constant of the protein from 4.50 to 1.35 N/m upon increasing the temperature from S to 45 degrees C. Interestingly, near-UV circular dichroism spectroscopy reveals a decrease in tertiary structure content while the overall secondary structure of the protein remains unchanged. Steady-state fluorescence and quenching studies on SUMO2 with a tryptophan mutation at the core (F6OW) show that the nonpolar environment of the tryptophan is unchanged and the protein core is inaccessible to the bulk solvent, in the same temperature range. We attribute the thermal softening observed in atomic force microscopy (AFM) experiments to the reduction in tertiary structure of SUMO2. Our results provide evidence for the importance of the intramolecular interactions at the protein core along with the beta-clamp or mechanical clamp in providing the mechanical resistance as well as in modulating the protein stiffness.
机译：尽管对蛋白质的热软化感兴趣，但它的机制细节远非理解。 β-克蛋白质具有紧凑的结构，它们是机械弹性的球状。通过末端β-股线之间的相互作用形成的β-夹或机械钳通常与蛋白质机械抗性相关。虽然之前的研究表明，温度可以扰乱蛋白质机械稳定性，但是不知道导致机械电阻降低的结构变化。这里，我们使用单分子力谱（SMF）研究了小泛素相关改性剂2（SUMO2）的温度依赖性机械稳定性，并使用集合实验相应的构象变化。 SMFS对SuMo2的多蛋白质的研究估计在从S至45摄氏度的温度增加到4.50至1.35n / m时估计蛋白质的弹簧常数的降低。有趣的是，接近UV圆形二色性谱谱显示第三级结构含量的降低虽然蛋白质的整体二级结构保持不变。在核心（F6OW）上具有色氨酸突变的Sumo2稳态荧光和猝灭研究表明，色氨酸的非极性环境不变，蛋白质核心在相同的温度范围内难以进入批量溶剂。我们将在原子力显微镜（AFM）实验中观察到的热软化，以减少SuMO2的三级结构。我们的研究结果为蛋白质芯的分子内相互作用以及β-夹或机械钳提供了提供机械阻力以及调节蛋白质刚度的表现提供了证据。

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