通过衰减全反射傅里叶变换红外光谱法检测白细胞介素-1β包涵体中的类天然二级结构
Nativelike secondary structure in interleukin-1 beta inclusion bodies by attenuated total reflectance FTIR.
作者信息
Oberg K, Chrunyk B A, Wetzel R, Fink A L
机构信息
Department of Chemistry and Biochemistry, University of California, Santa Cruz 95064.
出版信息
Biochemistry. 1994 Mar 8;33(9):2628-34. doi: 10.1021/bi00175a035.
Attenuated total reflectance FTIR has been used to study the structure of human interleukin-1 beta in inclusion bodies (IBs) and other aggregated forms. The secondary structure composition of native wild-type IL-1 beta determined by FTIR is in excellent agreement with that previously determined by crystallography and NMR: 52% beta-sheet, 25% loop/irregular structure, and 23% turn. Remarkably, IL-1 beta inclusion bodies exhibit secondary structural composition very similar to that of the native protein. The results indicate that the IBs form from a folding intermediate that has nativelike secondary structure. The secondary structure content of aggregated IL-1 beta, formed either in refolding or by thermal denaturation, was identical within experimental error to that of the IB, indicating that these aggregates were formed from intermediates with structures similar to that of the inclusion body.
衰减全反射傅里叶变换红外光谱（Attenuated total reflectance FTIR）已被用于研究人白细胞介素-1β在包涵体（IBs）和其他聚集形式中的结构。通过傅里叶变换红外光谱（FTIR）测定的天然野生型IL-1β的二级结构组成与先前通过晶体学和核磁共振（NMR）测定的结果高度一致：52%的β-折叠、25%的环/不规则结构和23%的转角。值得注意的是，IL-1β包涵体的二级结构组成与天然蛋白质非常相似。结果表明，包涵体由具有类似天然二级结构的折叠中间体形成。在复性或热变性过程中形成的聚集态IL-1β的二级结构含量在实验误差范围内与包涵体的二级结构含量相同，表明这些聚集体由结构类似于包涵体的中间体形成。
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