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一种分子磁体被限制在球形蛋白质的纳米笼中。

A molecular magnet confined in the nanocage of a globular protein.

机构信息

Unit for Nano Science and Technology, Department for Chemical, Biological and Macromolecular Sciences, S.N. Bose National Centre for Basic Sciences, Block JD, Sector III, Salt Lake, Kolkata 700098, India.

出版信息

Chemphyschem. 2010 Feb 1;11(2):389-93. doi: 10.1002/cphc.200900708.

Abstract

The effect of confinement and energy transfer on the dynamics of a molecular magnet, known as a model system to study quantum coherence, is investigated. For this purpose the well-known polyoxovanadate V(15)As(6)O(42)(H(2)O) (V(15)) is incorporated into a protein (human serum albumin, HSA) cavity. Due to a huge overlap of the optical absorption spectrum of V(15) with the emission spectrum of a fluorescence center of HSA (containing a single tryptophan residue), energy transfer is induced and probed by steady-state and time-resolved fluorescence. The geometrical coordination and the distance of the confined V(15) to the tryptophan moiety of HSA are investigated at various temperatures. This effect is used as a local probe for the thermal denaturation of the protein at elevated temperatures.

摘要

研究了限制和能量转移对分子磁体动力学的影响,分子磁体通常被用作研究量子相干性的模型体系。为此,将著名的多钒酸盐V(15)As(6)O(42)(H(2)O)(V(15))嵌入到蛋白质(人血清白蛋白,HSA)腔中。由于 V(15)的光吸收光谱与 HSA 的荧光中心(含有单个色氨酸残基)的发射光谱有很大的重叠,因此能量转移被诱导,并通过稳态和时间分辨荧光进行探测。在不同温度下,研究了受限 V(15)与 HSA 中色氨酸部分的几何配位和距离。这种效应可用作在高温下探测蛋白质热变性的局部探针。

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