LASER-EXCITED RAMAN SPECTROSCOPY OF BIOMOLECULES .1. NATIVE LYSOZYME AND ITS CONSTITUENT AMINO ACIDS
LASER-EXCITED RAMAN SPECTROSCOPY OF BIOMOLECULES .1. NATIVE LYSOZYME AND ITS CONSTITUENT AMINO ACIDS
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DOI：
10.1016/0022-2836(70)90208-1
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发表时间：
1970-01-01
影响因子：
5.6
通讯作者：
YU, NT
中科院分区：
文献类型：
--
作者：
LORD, RC;YU, NT
本文报道了一种简单的天然蛋白质--溶菌酶在水溶液中的激光激发拉曼光谱，并借助其组成氨基酸的光谱进行了部分解释。拉曼光谱应该是有用的，在提供直接证据有关的存在和蛋白质中的二硫键交联的数量，也可能是有用的，在研究的本地构象的C S S C基团。苯丙氨酸、色氨酸和酪氨酸的芳香族侧基产生非常强烈和尖锐的线。这些线对构象或聚集状态的变化不敏感。肽CONH基团在1660（酰胺I）和1260 cm−1（酰胺III）附近产生两条特征线。他们似乎是潜在的有用的变性引起的构象变化的评估。在800 ~ 1150 cm− 1范围内，由C <$C和C <$N伸缩振动产生的谱线也被认为是构象依赖的。
Laser-excited Raman spectra of a simple native protein, lysozyme, in aqueous solution are reported and partially interpreted with the help of the spectra of its constituent amino acids. Raman spectroscopy should be useful in providing direct evidence concerning the presence and number of disulfide cross-links in proteins, and may also be useful in studying the local conformation of the CSSC group. The aromatic side-groups of phenylalanine, tryptophan and tyrosine give rise to very intense and sharp lines. These lines are not sensitive to changes in conformation or state of aggregation. The peptide CONH group gives rise to two characteristic lines near 1660 (amide I) and 1260 cm−1(amide III). They appear to be potentially useful in assessment of conformational changes caused by denaturation. Lines in the region from 800 to 1150 cm−1arising from CC and CN stretching vibrations are also expected to be conformation-dependent.