Bewley T A, Levine H L, Wetzel R
Int J Pept Protein Res. 1982 Jul;20(1):93-6. doi: 10.1111/j.1399-3011.1982.tb02658.x.
The solution structure of human leukocyte (alpha) interferon-A (LeIF-A) purified from E. coli extracts was investigated by circular dichroism spectroscopy. At pH 8.2, the native molecule exhibits 40-70% alpha-helix and no clearly detectable beta-structure. The tertiary structure includes a closely-packed interior containing at least one tryptophan side-chain. Titration to pH 1.5 produces a partial loss of structural features which are rapidly regained on return to neutral pH.
通过圆二色光谱法研究了从大肠杆菌提取物中纯化得到的人白细胞(α)干扰素 -A(LeIF -A)的溶液结构。在pH 8.2时,天然分子呈现40 - 70%的α - 螺旋结构,且没有明显可检测到的β - 结构。其三级结构包括一个紧密堆积的内部,含有至少一个色氨酸侧链。滴定至pH 1.5会导致结构特征部分丧失,而回到中性pH时这些特征会迅速恢复。