蛋白质动力学转变与水合作用无关
The protein dynamical transition is independent of hydration
AI总结：
本研究通过太赫兹光谱和量热法证明，干态生物分子在无 hydration 条件下仍出现与蛋白质动力学转变相关的非谐运动，表明该转变不依赖水合作用。
摘要：
本研究采用太赫兹时域光谱和差示扫描量热法，研究了与溶剂效应解耦的生物分子动力学的角色。冻干蔗糖在温度升高时表现出持续增加的吸收，这是因为系统从势能景观的深最小值中涌现时，非谐激发开始启动，而在此最小值中谐波振动占主导。多肽杆菌肽和两种球状蛋白质——溶菌酶和人血清白蛋白——则表现出更复杂的温度依赖性。进一步分析聚焦于玻色峰下方和上方的光谱特征。我们发现了干态生物分子中非谐运动启动的证据，这些运动是部分展开和分子堵塞的特征。在无水合作用的情况下，观察到蛋白质分子在接近蛋白质动力学转变温度的温度下激活模式。在我们的实验中，未发现被推测促进生物功能的Fröhlich相干性的证据。
英文摘要：
Terahertz time-domain spectroscopy and differential scanning calorimetry were used to study the role of the dynamics of biomolecules decoupled from solvent effects. Lyophilised sucrose exhibited steadily increasing absorption with temperature as anharmonic excitations commence as the system emerges from a deep minimum of the potential energy landscape where harmonic vibrations dominate. The polypeptide bacitracin and two globular proteins, lysozyme and human serum albumin, showed a more complex temperature dependence. Further analysis focused on the spectral signature below and above the boson peak. We found evidence for the onset of anharmonic motions that are characteristic for partial unfolding and molecular jamming in the dry biomolecules. The activation of modes of the protein molecules at temperatures comparable to the protein dynamical transition temperature was observed in the absence of hydration. No evidence for Fröhlich coherence, postulated to facilitate biological function, was found in our experiments.
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