Cysteine conformation and sulfhydryl interactions in proteins and viruses. 3. Quantitative measurement of the Raman S-H band intensity and frequency.
Cysteine conformation and sulfhydryl interactions in proteins and viruses. 3. Quantitative measurement of the Raman S-H band intensity and frequency.
复制标题
蛋白质和病毒中的半胱氨酸构象和巯基相互作用。
DOI：
10.1016/s0006-3495(93)81172-x
复制
发表时间：
1993
影响因子：
3.4
通讯作者：
ThomasJr,GJ
中科院分区：
文献类型：
--
作者：
Tuma,R;Vohnik,S;Li,H;ThomasJr,GJ
典型蛋白质中半胱氨酸巯基（SH）基团的键拉伸振动在光谱区间2500-2600 cm-1内产生拉曼带，该区域不受蛋白质任何其他基本振动模式的干扰。与S-H拉伸振动相关的相对较高的拉曼横截面，振动频率对氢键相互作用和侧链构型的敏感性，以及拉曼强度对硫-硫酸盐平衡的依赖性，使拉曼SH带成为蛋白质巯基相互作用的潜在有价值的标记物，也是巯基参与硫-二硫氧化还原酶活性的独特指标。为了将拉曼光谱用于这些目的，需要精确和精确地测量拉曼SH波段剖面。我们在这里表明，使用与原位氮气拉伸振动相对应的拉曼波段作为定量强度和频率标准，可以达到所需的精度和准确度。N2波段的拉曼q分支中心位于2330.7 cm-1。
The bond stretching vibration of the cysteine sulfhydryl (SH) group in a typical protein generates a Raman band in the spectral interval 2500–2600 cm-1, a region devoid of interference from any other fundamental mode of vibration of the protein. The relatively high Raman cross section associated with the S-H stretching vibration, the sensitivity of the vibrational frequency to hydrogen bonding interactions and side chain configurations, and the dependence of the Raman intensity on thiol-thiolate equilibria, combine to make the Raman SH band a potentially valuable marker of protein sulfhydryl interactions and a unique indicator of sulfhydryl participation in thiol-disulfide oxidoreductase activity. In order to exploit Raman spectroscopy for these purposes, accurate and precise measurements of Raman SH band profiles are required. We show here that the required precision and accuracy can be achieved by use of the Raman band corresponding to the stretching vibration of in situ nitrogen gas as a quantitative intensity and frequency standard. The Raman Q-branch center of the N2 band occurs at 2330.7 cm-1.