Circular dichroism and optical rotatory dispersion of alpha-gliadin.

Circular dichroism and optical rotatory dispersion of alpha-gliadin.
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α-麦醇溶蛋白的圆二色性和旋光色散。

DOI:
10.1021/bi00851a023
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发表时间:
1968
期刊:
影响因子:
2.9
通讯作者:
William Gaffield
William Gaffield
中科院分区:
生物学3区
文献类型:
--
作者:
D. Kasarda;J. Bernardin;William Gaffield

文献摘要

被引文献

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Donald D. Kasarda、John E. Bernardin 和 William Gaffield 摘要:a-麦醇溶蛋白(一种小麦蛋白)的圆二色光谱是在 10-3 m HCl (pH 3)、" 5 m HCl (pH 5) 和 10" 5 m HC1 加 0.005 m KC1 (pH 5) 中测量的。频段为 222、208 和 ca。 191\μ表示存在某种螺旋结构。 pH 5 溶液在 222 µ 处的椭圆度为 11,300 (deg cm2)/dmole-1,表明其具有大约三分之一的螺旋结构。尽管在 pH 5 时添加少量盐时蛋白质会聚集,但与肽键相关的圆二色性没有发现相应的变化。我们推断当蛋白质聚集时没有发生重大构象变化。与侧链相关的带
Donald D. Kasarda, John E. Bernardin, and William Gaffield abstract: The circular dichroism spectrum of a-gliadin, a wheat protein, was measured in 10-3 m HC1 (pH 3)," 5 m HC1 (pH 5), and 10" 5 m HC1 plus 0.005 m KC1 (pH 5). Bands at 222, 208, and ca. 191\µ indicate the presence of some helical structure. The ellipticity 11,300 (deg cm2)/dmole-1 at 222 µ for pH 5 solutions suggests about one-third helicalstructure. Although the protein aggregates when a small amount of salt is added at pH 5, no corresponding change was found in the circular dichroism associated with the peptide bonds. We infer that no major conformational change occurs when the protein aggregates. Bands associated with side-chain