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首页> 外文期刊>Journal of Molecular Biology >Mechanical Unfolding of a Titin Ig Domain: Structure of Unfolding Intermediate Revealed by Combining AFM, Molecular Dynamics Simulations, NMR and Protein Engineering.
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Mechanical Unfolding of a Titin Ig Domain: Structure of Unfolding Intermediate Revealed by Combining AFM, Molecular Dynamics Simulations, NMR and Protein Engineering.

机译：Titin Ig域的机械展开：通过结合AFM，分子动力学模拟，NMR和蛋白质工程揭示了展开中间体的结构。

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摘要

The mechanical unfolding of an immunoglobulin domain from the human muscle protein titin (TI I27) has been shown to proceed via a metastable intermediate in which the A-strand is detached. The structure and properties of this intermediate are characterised in this study. A conservative destabilising mutation in the A-strand has no effect on the unfolding force, nor the dependence of the unfolding force on the pulling speed, indicating that the unfolding forces measured in an AFM experiment are those required for the unfolding of the intermediate and not the native state. A mutant of TI I27 with the A-strand deleted (TI I27-A) is studied by NMR and standard biophysical techniques, combined with protein engineering. Molecular dynamics simulations show TI I27-A to be a good model for the intermediate. It has a structure very similar to the native state, and is surprisingly stable. Comparison with a Phi-value analysis of the unfolding pathway clearly shows that the protein unfolds by a different pathway under an applied force than on addition of denaturant.
机译：已显示免疫球蛋白结构域从人肌肉蛋白效价蛋白（TI I27）的机械解链是通过亚稳态中间产物进行的，其中A链已分离。该研究表征了该中间体的结构和性质。 A链上保守的破坏稳定的突变对展开力没有影响，也没有展开力对拉速的依赖性，这表明在AFM实验中测得的展开力是中间体展开所需的力，而不是原始状态。通过NMR和标准生物物理技术结合蛋白质工程研究了缺失A链的TI I27突变体（TI I27-A）。分子动力学模拟表明TI I27-A是中间体的良好模型。它的结构与原始状态非常相似，并且非常稳定。与展开路径的Phi值分析的比较清楚地表明，与施加变性剂相比，在施加的力作用下蛋白质通过不同的途径展开。

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