Application of fluorescence spectroscopy for determining the structure and function of proteins.

Application of fluorescence spectroscopy for determining the structure and function of proteins.
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DOI:
10.1007/978-1-4899-1079-0_1
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发表时间:
1995
期刊:
Pharmaceutical biotechnology
影响因子:
--
通讯作者:
W. Jiskoot;V. Hlady;J. Naleway;J. Herron
W. Jiskoot;V. Hlady;J. Naleway;J. Herron
中科院分区:
其他
文献类型:
--
作者:
W. Jiskoot;V. Hlady;J. Naleway;J. Herron

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研究大分子结构的理想技术应具有原子级分辨率和高灵敏度,并能够动态地提供这些信息。不幸的是,目前没有一种技术能同时满足所有这些标准。例如,虽然x射线衍射可以提供原子级的信息,但它需要毫克级的材料,并且(在大多数情况下)只能产生时间平均结构。同样,核磁共振(NMR)光谱学需要毫克数量的蛋白质,并且只能提供大分子的不完整图像。此外,目前只能分辨相对较小的大分子(≤20,000 mol. wt)。另一方面,核磁共振光谱可以提供时域信息,如质子交换率和原子的振动运动。
The ideal technique to investigate the structure of macromolecules would feature both atomic-level resolution and high sensitivity and would be able to provide this information dynamically. Unfortunately, none of the present-day techniques satisfy all of these criteria simultaneously. For instance, while X-ray diffraction can provide atomic-level information, it requires milligram quantities of material and produces (in most cases) only a time-averaged structure. Likewise, nuclear magnetic resonance (NMR) spectroscopy requires milligram quantities of protein and provides only an incomplete picture of the macromolecule. Furthermore, only relatively small macromolecules (≤ 20,000 mol. wt.) can presently be resolved. On the other hand, NMR spectroscopy can provide information in the time domain, such as proton exchange rates and the vibrational motion of atoms.