Saito K, Sato Y, Edo K, Akiyama-Murai Y, Koide Y, Ishida N, Mizugaki M
Chem Pharm Bull (Tokyo). 1989 Nov;37(11):3078-82. doi: 10.1248/cpb.37.3078.
Characteristics of the secondary structure of neocarzinostatin apoprotein (apo-NCS) were examined by various means. Gaussian analysis of the Fourier-transform infrared (FT-IR) curve and curve-fitting of the circular dichroism (CD) spectrum for apo-NCS revealed that this peptide was abundant in beta-structures. In the presence of sodium dodecyl sulfate (SDS), the CD bands of NCS originating from phenylalanyl, tyrosyl, and cystinyl residues decreased, indicating a conformational change around the chromophore (CNS-chr). On the other hand, apo-NCS, in the SDS system, showed no change of these bands. We showed that the major parts of the protein moiety consist of beta-structures by measurements of the FT-IR and CD spectra of apo-NCS and a prediction of the secondary structure based on the amino acid sequence of the peptide. It seems that properties of the protein may be important to the hydrophobic interaction between NCS-chr and apo-NCS.
通过多种方法研究了新制癌菌素脱辅基蛋白（apo-NCS）二级结构的特征。对apo-NCS的傅里叶变换红外（FT-IR）曲线进行高斯分析以及对圆二色性（CD）光谱进行曲线拟合，结果表明该肽富含β-结构。在十二烷基硫酸钠（SDS）存在的情况下，源自苯丙氨酰基、酪氨酰基和胱氨酰基残基的NCS的CD谱带降低，表明发色团（CNS-chr）周围发生了构象变化。另一方面，在SDS体系中的apo-NCS这些谱带没有变化。通过对apo-NCS的FT-IR和CD光谱进行测量以及基于该肽的氨基酸序列对二级结构进行预测，我们表明蛋白质部分的主要部分由β-结构组成。蛋白质的性质似乎对NCS-chr与apo-NCS之间的疏水相互作用很重要。
