一种解释蛋白质圆二色光谱的新依据。
A new basis for interpreting the circular dichroic spectra of proteins.
作者信息
Saxena V P, Wetlaufer D B
出版信息
Proc Natl Acad Sci U S A. 1971 May;68(5):969-72. doi: 10.1073/pnas.68.5.969.
Abstract
Experimental circular dichroic (CD) spectra of three proteins have been combined with estimates of the content of peptide-chain structural modes obtained from x-ray diffraction studies of the same proteins. Solution of the simultaneous equations at a series of wavelengths permits the construction of a CD spectrum for each of three structural modes: alpha-helix, beta-structure, and the so-called "random". The CD spectra thus obtained are compared with those obtained from polypeptide models. The alpha-helical spectra from the two approaches are nearly congruent, the beta-structure spectra are in fair agreement, and the third forms agree qualitatively, but are substantially different quantitatively. Comparisons are made between the present approach and earlier approaches to interpreting protein CD spectra. Certain advantages of the present approach are indicated.
摘要
三种蛋白质的实验性圆二色光谱（CD）已与通过对相同蛋白质进行X射线衍射研究获得的肽链结构模式含量估计相结合。在一系列波长下求解联立方程，可以构建三种结构模式（α螺旋、β结构和所谓的“无规卷曲”）各自的CD光谱。由此获得的CD光谱与从多肽模型获得的光谱进行了比较。两种方法得到的α螺旋光谱几乎完全一致，β结构光谱基本相符，第三种形式在定性上一致，但在定量上有很大差异。对本方法与早期解释蛋白质CD光谱的方法进行了比较。指出了本方法的某些优点。
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