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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >Direct observation of protein folding in nanoenvironments using a molecular ruler
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Direct observation of protein folding in nanoenvironments using a molecular ruler

机译：使用分子尺直接观察纳米环境中的蛋白质折叠

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摘要

We observe folding of horse heart cytochrome c in various environments including nano-compartments (micelles and reverse micelles). Using picosecond-resolved Forster resonance energy transfer (FRET) dynamics of an extrinsic covalently attached probe dansyl donor) at the surface of the protein to a heme group (acceptor) embedded inside the protein, we measured angstrom-resolved donor-acceptor distances in the environments. The overall structural perturbations of the protein revealed from the FRET experiments are in close agreement with our circular dichroism (CD) and dynamic light scattering (DLS) studies on the protein in a variety of solution conditions. The change of segmental motion of the protein due to imposed restriction in the nano-compartments compared to that in bulk buffer is also revealed by temporal fluorescence anisotropy of the dansyl probe. (c) 2006 Elsevier B.V. All rights reserved.
机译：我们观察到在包括纳米隔室（胶束和反胶束）在内的各种环境中马心脏细胞色素c的折叠。使用皮秒分辨的外在的共价连接的探针dansyl供体的皮秒分辨的Forster共振能量转移（FRET）动力学（在蛋白质表面上嵌入到蛋白内部的血红素基团（受体）），我们测量了环境。 FRET实验揭示的蛋白质的整体结构扰动与我们在各种溶液条件下对蛋白质的圆二色性（CD）和动态光散射（DLS）研究非常一致。相比于整体缓冲液，由于在纳米隔室中施加了限制，蛋白质的分段运动变化也通过丹磺酰基探针的时间荧光各向异性来揭示。 （c）2006 Elsevier B.V.保留所有权利。

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