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Inelastic neutron scattering spectroscopy of amino acids

机译:氨基酸的非弹性中子散射光谱

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摘要

A combination of infrared, Raman and inelastic neutron scattering (INS) spectroscopies are used to provide complete vibrational spectra of several amino acids and dipeptides. The amino acids studied were glycine, alanine, glutamine, cysteine, methionine and phenylalanine and the dipeptides studied were Gly-Gln and Gly-Ala. The findings of this study have shown how the complementarity of infrared, Raman and INS spectroscopies can be exploited to provide complete vibrational spectra of amino acids and peptides. In particular, the strengths of INS spectroscopy are highlighted: the absence of selection rules, that hydrogenic motions are emphasised, the ready access to the low energy regime (<400 cm(-1)) and the straightforward calculation of intensities. In the future, it should be possible to apply this approach to the study of larger peptides as well as proteins.
机译:结合使用红外光谱,拉曼光谱和非弹性中子散射(INS)光谱技术来提供几种氨基酸和二肽的完整振动光谱。研究的氨基酸是甘氨酸,丙氨酸,谷氨酰胺,半胱氨酸,蛋氨酸和苯丙氨酸,研究的二肽是Gly-Gln和Gly-Ala。这项研究的结果表明,如何利用红外光谱,拉曼光谱和INS光谱学的互补性来提供氨基酸和多肽的完整振动光谱。特别要强调的是INS光谱学的优势:缺乏选择规则,强调氢运动,易于进入低能态(<400 cm(-1))和强度的简单计算。将来,应该有可能将这种方法应用于更大的肽以及蛋白质的研究。

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