Spectral pointillism of enhanced Raman scattering for accessing structural and conformational information on single protein
Spectral pointillism of enhanced Raman scattering for accessing structural and conformational information on single protein
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DOI：
10.1039/c6cp06667d
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发表时间：
2017-01-07
影响因子：
3.3
通讯作者：
Finot, Eric
中科院分区：
文献类型：
--
作者：
Clement, Jean-Emmanuel;Leray, Aymeric;Finot, Eric
在这一贡献中，我们提供了关于大单分子（如蛋白质）表面增强拉曼光谱（SERS）的时间波动的新见解。由于它们只能部分地适应小的活性体积，因此SERS分析被称为光谱点分析法，其中只有蛋白质子结构域被照亮，整个蛋白质景观是由连续的单个光谱动态构建的。通过将我们的方法应用于牛血清白蛋白，我们发现单个蛋白质亚域主要由三个不同的氨基酸组成。表面氨基酸如赖氨酸在蛋白质的开放形式中被优先检测到。单蛋白状态下色氨酸费米双重态的研究对蛋白质构象具有重要的指导意义。我们最后证明，光谱点点法能够将单个氨基酸与结构信息联系起来。
In this contribution, we provide new insights on the temporal fluctuations of surface enhanced Raman spectra (SERS) of large single molecules such as proteins. Because they can only fit partly into small active volume, SERS analysis is referred to spectral pointillism where only protein subdomains are shined and the whole protein landscape is built from the dynamics of successive individual spectra. By applying our approach on bovine serum albumin, we show that single protein subdomains are mostly comprised of three distinct amino acids. Surface amino acids such as lysine are preferentially detected in the open form of the protein. The investigation of the tryptophan Fermi doublet in the single protein regime is highly instructive on the protein conformation. We finally demonstrate that spectral pointillism enables to correlate individual amino acids with structural information.