Effects of hydrogen bonding and hydrophobic interactions on the ultraviolet resonance Raman intensities of indole ring vibrations
Effects of hydrogen bonding and hydrophobic interactions on the ultraviolet resonance Raman intensities of indole ring vibrations
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DOI：
10.1246/bcsj.71.851
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发表时间：
1998-04-01
影响因子：
4
通讯作者：
Takeuchi, H
中科院分区：
文献类型：
--
作者：
Matsuno, M;Takeuchi, H
研究了不同溶剂性质溶液中吲哚环振动的紫外共振拉曼强度，建立了吲哚环振动强度与环境之间的关系。吲哚环是氨基酸色氨酸的主要侧链成分。当吲哚NH位与疏水环境中的质子受体氢键时，通过与B-b电子跃迁共振增强的每个拉曼光谱都具有最高的强度。另一方面，当吲哚环不是氢键时，通过与L-α跃迁共振而获得强度的拉曼光谱最强。虽然拉曼强度的这些变化分别是由于B-b和L-a吸收的小的红移和蓝移造成的，但拉曼强度的变化远远大于紫外吸收光谱的变化。因此，紫外共振拉曼强度有望成为蛋白质中色氨酸残基氢键和疏水相互作用的有用标记。
UV resonance Raman intensities of indole ring vibrations were examined in solutions of different solvent properties to establish the correlation between the intensity and the environment of the indole ring, the main side-chain component of amino acid tryptophan. Each of the Raman bands that are enhanced through resonance with the B-b electronic transition gives the highest intensity when the indole NH site is hydrogen-bonded with a proton acceptor in hydrophobic environments. On the other hand, the Raman bands that gain intensity through resonance with the L-a transition are most enhanced when the indole ring is not hydrogen-bonded. Although these changes in Raman intensity result from small red and blue shifts of the B-b and L-a absorptions, respectively, the Raman intensity changes are much greater than the changes in UV absorption spectra. UV resonance Raman intensities are thus expected to be useful markers of hydrogen bonding and hydrophobic interactions of tryptophan residues in proteins.