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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Identifying the subproteome of kinetically stable proteins via diagonal 2D SDS/PAGE
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Identifying the subproteome of kinetically stable proteins via diagonal 2D SDS/PAGE

机译：通过对角2D SDS / PAGE鉴定动力学稳定蛋白的亚蛋白质组

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摘要

Most proteins are in equilibrium with partially and globally unfolded conformations. In contrast, kinetically stable proteins (KSPs) are trapped by an energy barrier in a specific state, unable to transiently sample other conformations. Among many potential roles, it appears that kinetic stability (KS) is a feature used by nature to allow proteins to maintain activity under harsh conditions and to preserve the structure of proteins that are prone to misfolding. The biological and pathological significance of KS remains poorly understood because of the lack of simple experimental methods to identify this property and its infrequent occurrence in proteins. Based on our previous correlation between KS and a protein's resistance to the denaturing detergent SDS, we show here the application of a diagonal 2D (D2D) SDS/PAGE assay to identify KSPs in complex mixtures. We applied this method to the lysate of Escherichia coli and upon proteomics analysis have identified 50 nonredundant proteins that were SDS-resistant (i.e., kinetically stable). Structural and functional analyses of a subset (44) of these proteins with known 3D structure revealed some potential structural and functional biases toward and against KS. This simple D2D SDS/PAGE assay will allow the widespread investigation rnof KS, including the proteomics-levei identification of KSPs in different systems, potentially leading to a better understanding of the biological and pathological significance of this intriguing property of proteins.
机译：大多数蛋白质与部分和全局展开的构象处于平衡状态。相比之下，动力学稳定的蛋白质（KSP）在特定状态下被能垒捕获，无法瞬时采样其他构象。在许多潜在作用中，似乎动态稳定性（KS）是自然界所使用的功能，可让蛋白质在苛刻条件下保持活性并保留易于错误折叠的蛋白质结构。由于缺乏简单的实验方法来鉴定该特性及其在蛋白质中的罕见性，KS的生物学和病理学意义仍然知之甚少。基于我们先前在KS与蛋白质对变性洗涤剂SDS的抗性之间的相关性，我们在这里展示了对角2D（D2D）SDS / PAGE分析法在复杂混合物中鉴定KSP的应用。我们将此方法应用于大肠杆菌的裂解物中，通过蛋白质组学分析，已鉴定出50种对SDS具有抗性（即动力学稳定）的非冗余蛋白。对具有已知3D结构的这些蛋白质的一部分（44）进行结构和功能分析，发现它们对KS和针对KS有一些潜在的结构和功能偏差。这种简单的D2D SDS / PAGE测定法将使KS广泛的研究成为可能，包括蛋白质组学方面的不同系统中KSP的鉴定，从而有可能使人们更好地了解这种蛋白质有趣特性的生物学和病理学意义。

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