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Out-of-Equilibrium Collective Oscillation as Phonon Condensation in a Model Protein

机译：在模型蛋白中均衡的集体振荡作为声子凝结

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We describe the activation of out-of-equilibrium collective oscillations of a macromolecule as a classical phonon condensation phenomenon. If a macromolecule is modeled as an open system—that is, it is subjected to an external energy supply and is in contact with a thermal bath to dissipate the excess energy—the internal nonlinear couplings among the normal modes make the system undergo a nonequilibrium phase transition when the energy input rate exceeds a threshold value. This transition takes place between a state where the energy is incoherently distributed among the normal modes and a state where the input energy is channeled into the lowest-frequency mode entailing a coherent oscillation of the entire molecule. The model put forward in the present work is derived as the classical counterpart of a quantum model proposed a long time ago by Fr?hlich in an attempt to explain the huge speed of enzymatic reactions. We show that such a phenomenon is actually possible. Two different and complementary THz near-field spectroscopic techniques—a plasmonic rectenna and a microwire near-field probe—have been used in two different labs to eliminate artifacts. By considering an aqueous solution of a model protein, the bovine serum albumin, we find that this protein displays a remarkable absorption feature around 0.314?THz, when driven in a stationary out-of-thermal equilibrium state by means of optical pumping. The experimental outcomes are in very good qualitative agreement with the theory developed in the first part of the paper and in excellent quantitative agreement with the theoretical result, allowing us to identify the observed spectral feature with a collective oscillation of the entire molecule.
机译：我们描述了激活大分子的平衡集体振荡作为经典的声音凝结现象。如果MacromoleCule被建模为开放系统 - 即，它经受外部能量供应，并且与热浴接触以消散过量的能量 - 正常模式中的内部非线性耦合使得系统经历非支出阶段当能量输入速率超过阈值时转换。这种转变在能量在正常模式中分布在正常模式中的状态和输入能量被引导到引起整个分子的相干振荡中的最低频率模式之间的状态之间进行。在本作中提出的模型被推导出在很久以前提出的Quantum模型的经典对应物，以试图解释酶促反应的巨大速度。我们表明这种现象实际上是可能的。两种不同和互补的THz近场光谱技术 - 一种等离子体indenna和微线近场探针 - 已被用于两种不同的实验室以消除伪影。通过考虑模型蛋白的水溶液，牛血清白蛋白，我们发现该蛋白质在通过光学泵送在静止外平衡状态下驱动时，该蛋白质在0.314〜THz上显示出显着的吸收特征。实验结果与本文第一部分和卓越的定量协议具有非常良好的定性协议，以及与理论结果的良好定量协议，允许我们用整个分子的集体振荡识别观察到的光谱特征。

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