Extending circular dichroism spectra into the vacuum UV and its application to proteins.
Extending circular dichroism spectra into the vacuum UV and its application to proteins.
复制标题
将圆二色性光谱扩展到真空紫外及其在蛋白质中的应用。
DOI：
10.1111/j.1751-1097.1986.tb04669.x
复制
发表时间：
1986
影响因子：
3.3
通讯作者：
JohnsonJr,WC
中科院分区：
文献类型：
--
作者：
JohnsonJr,WC
在真空紫外区测量的圆二色性（CD）光谱提供了必要的信息，这种技术，以实现其潜力。在蛋白质的情况下，测量到184 nm或更低的CD光谱可以分析二级结构：广义逆使这种分析特别简单。以表格形式给出了α螺旋、反平行β折叠、平行β折叠、β转角和“其他”结构的广义逆。当每个逆的点积与蛋白质的数字化光谱一起取得时，预测相应二级结构的量。然而，蛋白质CD光谱截断以上184 nm给出太少的信息，给出可靠的分析。此外，添加约束只会使问题复杂化，因为不可靠的分析现在看起来很好。
Circular dichroism (CD) spectra measured into the vacuum UV region provide information necessary for this technique to fulfill its potential. In the case of proteins, CD spectra measured to 184 nm or below can be analyzed for secondary structure: generalized inverses make such analyses particularly simple. Generalized inverses for α‐helix, anti‐parallel β‐sheet, parallel β‐sheet, β‐turn, and “other” structures are given in tabular form. When the dot product of each inverse is taken with the digitized spectrum of a protein, the amount of corresponding secondary structure is predicted. However, protein CD spectra truncated above 184 nm give too little information to give reliable analyses. Furthermore, adding constraints only complicates this problem because unreliable analyses now appear good.