DETERMINATION OF HELIX AND BETA-FORM OF PROTEINS IN AQUEOUS-SOLUTION BY CIRCULAR-DICHROISM
DETERMINATION OF HELIX AND BETA-FORM OF PROTEINS IN AQUEOUS-SOLUTION BY CIRCULAR-DICHROISM
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DOI：
10.1021/bi00713a027
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发表时间：
1974-01-01
期刊：
影响因子：
2.9
通讯作者：
CHAU, KH
中科院分区：
文献类型：
--
作者：
CHEN, YH;YANG, JT;CHAU, KH
摘要：任一波长下蛋白质的圆二色性（CD）可表示为X=/hAh”+/ß ß+/rAr(1)。f是螺旋型（）、β型和无序型(R)的分数。ft是指蛋白质分子中每个螺旋段的平均肽单位数。用最小二乘法从已知的5种或8种蛋白质的CD光谱中确定了A参数。反过来，它们可以用来估计蛋白质的/h和/ß，通过拟合其CD光谱（低于245 nm）与eq 1。8种蛋白质的测试结果良好，前提是蛋白质的ñ接近参考蛋白质的总体ñ（约10）。这种对所有蛋白质的单一ñ的限制可以通过引入
CHEN, YANG, AND CHAU abstract: The circular dichroism (CD) of a protein at any wavelength can be expressed as X=/hAh"+/ß ß+/rAr (1). The f s are the fractions of helix (), ß form, and unordered form (R). ft refers to the average number of peptide units per helical segment in a protein molecule. The A parameters are determined from the CD spectra of five or eight proteins of known f s, using a least-squares method. They, in turn, can be used to estimate the/h and/ß of a protein by fitting its CD spectrum (below 245 nm) with eq 1. Results of tests on eight proteins are good, provided that the ñ of the proteins is close to the overall ñ of the reference proteins (around 10). This restriction of a single ñ for all proteins can be removed by introducing