非对称环境诱导自旋链中的蛋白质类弛豫
Asymmetric environment induces protein-like relaxation in spin chain
摘要：
蛋白质是氨基酸链，其根据热和化学环境条件扩散折叠或展开。虽然复杂的模型解释了真实蛋白质的详细方面，但找到将蛋白质动力学统一到一般开链松弛的特征仍然具有挑战性。最小挫折原则是实现这一目标的关键一步，揭示了蛋白质和自旋玻璃之间的基本联系。在这里，我们寻找蛋白质类松弛的出现在开放的自旋链超越有效域的最小挫折原则，专注于系统的哈密顿系统的作用，而不是挫折。我们发现，强不对称的耦合之间的每个自旋到其周围环境意味着密切相似的蛋白质折叠和展开动力学。也就是说，不对称浴可以（i）阻止系统找到其最小能量状态，即使在系统的哈密顿量中完全没有能量挫折的情况下，以及（ii）激发系统类似于热变性和化学变性之间的众所周知的区别。
英文摘要：
Proteins are aminoacid chains that diffusively fold or unfold depending on the thermal and chemical environmental conditions. While sophisticated models account for detailed aspects of real proteins, finding traits that unify protein dynamics to general open chains relaxation is still challenging. The principle of minimal frustration represents a key step towards this goal, revealing a fundamental link between proteins and spin glasses. Here, we search for the emergence of protein-like relaxation in open spin chains by going beyond the validity domain of the minimal frustration principle as to focus on the role of system-environment interactions rather than on frustration in the system's Hamiltonian. We find that strong asymmetries between the couplings of each spin to its immediate surroundings imply close similarities to protein folding and unfolding dynamics. Namely, an asymmetric bath can (i) block the system from finding its minimum energy state, even in the complete absence of energetic frustration in the system's Hamiltonian, and (ii) excite the system resembling the well-known distinction between thermal and chemical denaturations.
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