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A donor-acceptor pair for the real time study of vibrational energy transfer in proteins

机译：供体-受体对，用于实时研究蛋白质中的振动能量转移

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Vibrational energy transfer (VET) is believed to play an important role in protein function. Theoretical studies predict highly directional, anisotropic VET in proteins. Distinct energy transfer pathways which connect distant functional sites in proteins have been proposed by simulations, indicating a function in allosteric communication. Experimental evidence for such pathways, however, is lacking, in small molecules, ultrafast vibrational pump-probe spectroscopy has been used to investigate VET between different parts of a molecule in great detail. Here, we address the requirements for extending this powerful approach to proteins and present a protein-compatible donor-acceptor pair for the real time investigation of VET. This VET pair consists of two non-native amino acids, β-(1-azulenyl)-atanine and azidohomoalanine, which can be positioned site-specifically and are found to be very well suited for spectroscopic studies of VET. Important for the study of proteins, co-translational incorporation of each of the amino acids has been demonstrated before using mutually independent approaches of protein engineering. We investigated the performance of the proposed VET pair in a model peptide which is designed to contain additional characteristic vibrational modes frequently used in infrared spectroscopy of proteins. Despite a larger inter-residue distance, we find that our VET acceptor generates a major signal that is easily observed compared to the other vibrational modes in the congested parts of the spectrum. We find sufficient signal size at concentrations compatible with proteins and over distances that will allow tracking of energy flow along predicted transfer pathways.
机译：振动能量转移（VET）被认为在蛋白质功能中起重要作用。理论研究预测蛋白质中具有高度定向性的各向异性VET。通过模拟已经提出了连接蛋白质中远距离功能位点的不同能量转移途径，这表明了变构通讯中的功能。然而，在小分子中，缺乏这种途径的实验证据，超快振动泵浦探针光谱已用于详细研究分子不同部分之间的VET。在这里，我们解决了将这种强大的方法扩展到蛋白质的要求，并提出了一种蛋白质相容的供体-受体对，用于VET的实时研究。该VET对由两个非天然氨基酸β-（1-氮杂烯基）-腺嘌呤和叠氮高丙氨酸组成，它们可以在位点特异性定位，非常适合用于VET的光谱研究。对于蛋白质研究很重要，在使用相互独立的蛋白质工程方法之前，已经证明了每种氨基酸的共翻译结合。我们在模型肽中研究了提议的VET对的性能，该模型肽设计为包含蛋白质红外光谱中经常使用的其他特征振动模式。尽管残基之间的距离较大，但我们发现，与频谱拥挤部分中的其他振动模式相比，我们的VET受体产生的主要信号很容易观察到。我们发现在与蛋白质相容的浓度和远距离范围内足够的信号大小，这将允许跟踪沿着预测的传递途径的能量流。

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