Residue-Specific Conformational Heterogeneity of Proline-Rich Sequences Uncovered via Infrared Spectroscopy
Residue-Specific Conformational Heterogeneity of Proline-Rich Sequences Uncovered via Infrared Spectroscopy
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DOI：
10.1021/acs.analchem.8b03813
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发表时间：
2018-12-18
影响因子：
7.4
通讯作者：
Thielges, Megan C.
中科院分区：
文献类型：
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作者：
Bukowski, Gregory S.;Thielges, Megan C.
构象异质性是理解蛋白质功能的关键，但具有挑战性的量化。实验方法，可以提供足够的时间和空间分辨率，以测量甚至快速相互转换状态在特定位置的蛋白质是必要的，以充分阐明构象异质性和动态功能的贡献。红外光谱与碳氘键的引入相结合，提供了其环境的频率分辨探针，可以快速发现具有残基特异性细节的相互转换状态。使用这种方法，我们量化与不同脯氨酸骨架构象相关的富含脯氨酸的肽的构象异质性，以及揭示它们对序列上下文的依赖性。
Conformational heterogeneity is critical to understanding protein function but challenging to quantify. Experimental approaches that can provide sufficient temporal and spatial resolution to measure even rapidly interconverting states at specific locations in proteins are needed to fully elucidate the contribution of conformational heterogeneity and dynamics to function. Infrared spectroscopy in combination with the introduction of carbon deuterium bonds, which provide frequency-resolved probes of their environments, can uncover rapidly interconverting states with residue-specific detail. Using this approach, we quantify conformational heterogeneity of proline-rich peptides associated with different proline backbone conformations, as well as reveal their dependence on the sequence context.