Kunitz 领域 1 人的织物因素 pathwayinhibitor-2 (hTFPI-2/KD1 ) 的符合构造被 Fourier 变换学习了红外线的光谱学,圆形的二色性,和拉曼光谱学。hTFPI-2/KD1 在详细 conformational 揭示的 Fouriertransform 红外线的光谱学,圆形的二色性和拉曼光谱学观察的激烈的蛋白质改变的 25 ° C .The 包含了近似 17%alpha-helices,24% 贝它海滨, 46% 随机的卷, 13% 贝它拐弯,和二种二硫键(gggand tgt ) ,这被发现那 hTFPI-2/KDlwas 热地稳定。然而, KD1 能在高温度形成一种中间的形式,当温度被降低时,然后回到它的正常符合构造。活动试金也证明 thathTFPI-2/KDl 能在为 5min 被加热到 80 ° C 以后在胞质素上保留它的禁止的活动。
The conformation of Kunitz domain 1 of human tissue factor pathway inhibitor-2 (hTFPI-2/KD 1) has been studied by Fourier transform infrared spectroscopy, circular dichroism, and Raman spectroscopy. It was found that hTFPI-2/KDI contained approximately 17% α-helices, 24% β-strands, 46% random coils, 13% α-turns, and two kinds of disulfide bonds (ggg and tgt) at 25 ℃. The detailed conformational changes of the heated protein observed by Fourier transform infrared spectroscopy, circular dichroism and Raman spectroscopy revealed that hTFPI-2/KD 1 was thermally stable. However, KD 1 could form an intermediate form at high temperature, then return to its normal conformation when the temperature was lowered. Activity assays also showed that hTFPI-2/KD 1 was able to keep its inhibitory activity on plasmin after being heated to 80 ℃ for 5 min.