Synchrotron X-ray footprinting as a method to visualize water in proteins.
Synchrotron X-ray footprinting as a method to visualize water in proteins.
复制标题
同步加速器 X 射线足迹法是一种可视化蛋白质中水的方法。
DOI：
10.1107/s1600577516009024
复制
发表时间：
2016-09-01
影响因子：
2.5
通讯作者：
Ralston CY
中科院分区：
文献类型：
--
作者：
Gupta S;Feng J;Chan LJ;Petzold CJ;Ralston CY
绝大多数的生物分子过程是由结合水控制的，并且没有直接的方法来解决与蛋白质-水相互作用相关的重要生物学问题。在这篇文章中，已取得的进展，在同步辐射为基础的辐解标记和质谱技术的结合沃茨的识别和表征的作用，在蛋白质构象变化的高度的空间和时间分辨率进行了总结。绝大多数生物分子过程都是由水的相互作用控制或促进的。在酶、调节蛋白、膜结合受体和离子通道中，与功能重要的残基结合的水形成氢键网络，构成大分子作用机制的基础。高分辨率的X射线结构通常很难获得许多这些类别的蛋白质，因为样品条件，如洗涤剂的必要性，往往阻碍结晶。其他生物物理技术，如中子散射，核磁共振和傅里叶变换红外光谱是有用的研究内部水，虽然每个都有自己的优点和缺点，往往需要一个混合的方法来解决重要的生物学问题与蛋白质-水的相互作用。需要更多研究的一个主要领域是研究存在于空腔和通道中的结合水分子，其通常涉及受体、转运蛋白和离子通道蛋白的结构和功能方面。近年来，基于同步辐射的辐射标记和质谱技术在识别结合沃茨和表征水在蛋白质构象变化中的作用方面取得了重大进展，具有高度的空间和时间分辨率。在这里讨论了这种方法用于研究水与蛋白质相互作用的最新发展和未来能力及其与其他基于同步加速器的方法的协同作用。
The vast majority of biomolecular processes are controlled by the bound water and there is no direct method to address the important biological problems associated with protein–water interactions. In this article, the progress that has been made in synchrotron-based radiolytic labeling and mass spectroscopy techniques for both the identification of bound waters and for characterizing the role of water in protein conformational changes at a high degree of spatial and temporal resolution are summarized. The vast majority of biomolecular processes are controlled or facilitated by water interactions. In enzymes, regulatory proteins, membrane-bound receptors and ion-channels, water bound to functionally important residues creates hydrogen-bonding networks that underlie the mechanism of action of the macromolecule. High-resolution X-ray structures are often difficult to obtain with many of these classes of proteins because sample conditions, such as the necessity of detergents, often impede crystallization. Other biophysical techniques such as neutron scattering, nuclear magnetic resonance and Fourier transform infrared spectroscopy are useful for studying internal water, though each has its own advantages and drawbacks, and often a hybrid approach is required to address important biological problems associated with protein–water interactions. One major area requiring more investigation is the study of bound water molecules which reside in cavities and channels and which are often involved in both the structural and functional aspects of receptor, transporter and ion channel proteins. In recent years, significant progress has been made in synchrotron-based radiolytic labeling and mass spectroscopy techniques for both the identification of bound waters and for characterizing the role of water in protein conformational changes at a high degree of spatial and temporal resolution. Here the latest developments and future capabilities of this method for investigating water–protein interactions and its synergy with other synchrotron-based methods are discussed.