Department of Chemistry, Yale University, New Haven, Connecticut 06520, United States.
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520, United States.
J Phys Chem B. 2023 Mar 23;127(11):2418-2429. doi: 10.1021/acs.jpcb.3c00217. Epub 2023 Mar 14.
We develop an electrostatic map for the vibrational NH stretch (amide A) of the protein backbone with a focus on vibrational chiral sum frequency generation spectroscopy (chiral SFG). Chiral SFG has been used to characterize protein secondary structure at interfaces using the NH stretch and to investigate chiral water superstructures around proteins using the OH stretch. Interpretation of spectra has been complicated because the NH stretch and OH stretch overlap spectrally. Although an electrostatic map for water OH developed by Skinner and co-workers was used previously to calculate the chiral SFG response of water structures around proteins, a map for protein NH that is directly responsive to biological complexity has yet to be developed. Here, we develop such a map, linking the local electric field to vibrational frequencies and transition dipoles. We apply the map to two protein systems and achieve much better agreement with experiment than was possible in our previous studies. We show that couplings between NH and OH vibrations are crucial to the line shape, which informs the interpretation of chiral SFG spectra, and that the chiral NH stretch response is sensitive to small differences in structure. This work increases the utility of the NH stretch in biomolecular spectroscopy.
我们开发了一个静电图谱,用于研究蛋白质骨架的振动 NH 伸缩(酰胺 A),重点是振动手性和频产生光谱学(手性 SFG)。手性 SFG 已被用于使用 NH 伸缩来表征界面处的蛋白质二级结构,并使用 OH 伸缩来研究蛋白质周围的手性水超结构。由于 NH 伸缩和 OH 伸缩在光谱上重叠,因此对光谱的解释变得复杂。尽管 Skinner 及其同事之前曾使用水 OH 的静电图谱来计算蛋白质周围水结构的手性 SFG 响应,但尚未开发出直接响应生物复杂性的蛋白质 NH 图谱。在这里,我们开发了这样一个图谱,将局部电场与振动频率和跃迁偶极子联系起来。我们将该图谱应用于两个蛋白质系统,并实现了比我们之前的研究更好的实验一致性。我们表明,NH 和 OH 振动之间的耦合对线形有至关重要的影响,这为手性 SFG 光谱的解释提供了信息,并且手性 NH 伸缩响应对结构的微小差异敏感。这项工作增加了 NH 伸缩在生物分子光谱学中的应用。