Natural and Artificial Proteins Containing Cadmium
Natural and Artificial Proteins Containing Cadmium
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DOI：
10.1007/978-94-007-5179-8_10
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发表时间：
2013-01-01
期刊：
影响因子：
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通讯作者：
Pecoraro, Vincent L.
中科院分区：
文献类型：
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作者：
Peacock, Anna F. A.;Pecoraro, Vincent L.
本章介绍了一种使用设计的蛋白质来了解结合 Cd(II) 的蛋白质的结构、光谱和动力学的方法。我们将展示基于母肽 TRI (Ac-G(LKALEEK)(4)G-NH2) 或 GRAND (Ac-G(LKALEEK)(5)G-NH2) 的三链卷曲线圈 (3SCC) 对于理解 Cd(II) 如何与蛋白质中富含硫醇盐的环境结合至关重要。给出了相关物理性质的示例，例如与结构相关的结合常数或去质子化常数。我们提出了一个尺度，将 Cd-113 NMR 化学位移与从 Cd-111m PAC 实验中提取的结构联系起来。此外，我们描述了有助于从蛋白质螺旋界面运输到螺旋束疏水内部的运动过程。这些研究有助于阐明 Cd(II) 与金属调节基因表达和解毒相关的化学性质。
This chapter describes an approach using designed proteins to understand the structure, spectroscopy, and dynamics of proteins that bind Cd(II). We will show that three-stranded coiled coils (3SCCs) based on the parent peptides TRI (Ac-G(LKALEEK)(4)G-NH2) or GRAND (Ac-G(LKALEEK)(5)G-NH2) have been essential for understanding how Cd(II) binds to thiolate-rich environments in proteins. Examples are given correlating physical properties such as the binding constants or deprotonation constants relating to structure. We present a scale that relates Cd-113 NMR chemical shifts to structures extracted from Cd-111m PAC experiments. In addition, we describe motional processes that help transport from the helical interface of proteins into the hydrophobic interior of helical bundles. These studies help clarify the chemistry of Cd(II) in relation to metal-regulated gene expression and detoxification.