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Terahertz Spectroscopy to Determine Cold Shock Protein Stability Upon Solvation and Evaporation—A Molecular Dynamics Study
IEEE Transactions on Terahertz Science and Technology ( IF 3.2 ) Pub Date : 2017-03-01 , DOI: 10.1109/tthz.2016.2637380
Saravana Prakash Thirumuruganandham 1 , Edgar A Gómez 2 , Shanmugamurthy Lakshmanan 3, 4 , Michael R Hamblin 3, 4
Affiliation  

Infrared (IR) and terahertz (THz) spectroscopy simulations were carried out using CHARMM35b2 to determine protein stability. The stabilities of three hyperthermophilic cold shock proteins (Csps) originating from mesophiles, thermophiles, and hyper-thermophiles, respectively, were investigated in this study. The three different Csps were investigated by normal-mode analysis and molecular dynamics simulation of THz spectra using the Hessian matrix for solvated systems, interpreted in the harmonic approximation at optimum near-melting temperatures of each homologue, by incorporating differences in the hydrous and anhydrous states of the Csps. The results show slight variations in the large-scale protein motion. However, the IR spectra of Csps observed at the low-frequency saddle surface region, clearly distinguishes the thermophilic and mesophilic proteins based on their stability. Further studies on protein stability employing low-frequency collective modes have the potential to reveal functionally important conformational changes that are biologically significant.

中文翻译:

太赫兹光谱测定溶剂化和蒸发时冷激蛋白的稳定性——分子动力学研究

使用 CHARMM35b2 进行红外 (IR) 和太赫兹 (THz) 光谱模拟以确定蛋白质稳定性。本研究分别研究了源自嗜温菌、嗜热菌和超嗜热菌的三种超嗜热冷休克蛋白 (Csps) 的稳定性。通过使用溶剂化系统的 Hessian 矩阵的太赫兹光谱的正态模式分析和分子动力学模拟研究了三种不同的 Csps,通过结合含水和无水状态的差异,在每个同系物的最佳近熔化温度下的谐波近似中解释的 Csps。结果显示大规模蛋白质运动的轻微变化。然而,在低频鞍形表面区域观察到的 Csps 的红外光谱,根据它们的稳定性清楚地区分嗜热蛋白和嗜温蛋白。采用低频集体模式对蛋白质稳定性的进一步研究有可能揭示具有生物学意义的重要功能构象变化。
更新日期:2017-03-01
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