Raman spectroscopy of proteins and their assemblies.

Raman spectroscopy of proteins and their assemblies.
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蛋白质及其组装体的拉曼光谱。

DOI:
10.1007/978-1-4899-1727-0_3
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发表时间:
1995
期刊:
Sub-cellular biochemistry.
影响因子:
--
通讯作者:
ThomasJr,GJ
ThomasJr,GJ
中科院分区:
--
文献类型:
--
作者:
Miura,T;ThomasJr,GJ

文献摘要

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激光拉曼光谱学与红外光谱学一样,是一种通过测量分子振动的能量(频率)来确定分子结构的方法。虽然这两种方法在辐射和物质之间的相互作用机制上有着根本的不同,但在这两种情况下都可以得到由许多离散带组成的振动光谱,其频率和强度由运动中的核质量、平衡分子几何形状和分子力场决定。对于生物应用,拉曼相对于红外光谱的重要优点是水(H2O和D2 O两者)在拉曼效应中的虚拟透明性。这大大简化了水溶液的分析,并促进了氢同位素交换现象的研究。分子几何形状的变化--特别是生物大分子的构象转变特征--可以在拉曼谱带位置产生大的位移,通常称为频移。使该技术在蛋白质二级结构的诊断,
Laser Raman spectroscopy, like infrared spectroscopy, is a method for determining molecular structure by measuring the energies (frequencies) of molecular vibrations. Although the two methods differ fundamentally in the mechanisms of interaction between radiation and matter, one obtains in both cases a vibrational spectrum consisting of a number of discrete bands, the frequencies and intensities of which are determined by the nuclear masses in motion, the equilibrium molecular geometry, and the molecular force field. An important advantage of Raman over infrared spectroscopy for biological applications is the virtual transparency of water (both H20 and D20) in the Raman effect. This greatly simplifies the analysis of aqueous solutions and facilitates the investigation of hydrogen-isotope exchange phenomena. Changes in molecular geometry-particularly the conformational transitions characteristic of biological macromolecules-can produce large shifts in Raman band positions, often referred to asfrequency shifts. empowering the technique in the diagnosis of protein secondary structure, determination of