Wei J A, Lin Y Z, Zhou J M, Tsou C L
National Laboratory of Biomacromolecules, Institute of Biophysics, Academia Sinica, Beijing, China.
Biochim Biophys Acta. 1991 Oct 11;1080(1):29-33. doi: 10.1016/0167-4838(91)90107-b.
The amide I bands of the deconvolved FTIR spectrum of bovine insulin, despentapeptide (B26-B30) insulin and desoctapeptide (B23-B30) insulin in D2O solution have been assigned to alpha-helix, the 3(10) helix, irregular helix, extended chains, beta-turns and other secondary structures. From the peak areas the relative contents of these structures obtained are in general agreement with those calculated from the known structures of porcine insulin and DPI in the crystalline state. The main difference in the structure of DOI with those of insulin and DPI is the shortening of the helix segment and an extended chain for the C terminal segment in the B chain.
已将重水（D₂O）溶液中牛胰岛素、去五肽（B26 - B30）胰岛素和去八肽（B23 - B30）胰岛素的去卷积傅里叶变换红外光谱（FTIR）的酰胺I带归属为α - 螺旋、3(10)螺旋、不规则螺旋、伸展链、β - 转角和其他二级结构。从峰面积得到的这些结构的相对含量与根据猪胰岛素和结晶态去五肽胰岛素（DPI）的已知结构计算得到的结果总体一致。去八肽胰岛素（DOI）与胰岛素和DPI在结构上的主要差异在于螺旋片段缩短以及B链C末端片段出现伸展链。
