摘要
本文利用拉曼光谱分析技术,对纯化后的螺旋藻C藻蓝蛋白(CPC)分子,在0075mol/L盐溶液中的空间结构进行了分析。本文认为CPC的脱辅蛋白空间构象在此溶液和10℃条件下是α螺旋与β回转结构。“暴露的”酪氨酸占44%;色氨酸也处于部份“暴露”状态;β111的半胱氨酸不参与硫醚键的形成,有自由的CS单键伸缩振动模;谱中没有二硫键的存在。
The Raman spectroscopic analysis method is employed to determine the spatial structural properties in the apoprotein of the light harvesting biliprotein C phycocyanin (i.e. C PC) from the cyanobacterium Spirulina platensis. In test condition of 0.075 mol/L NaCl solution and 10℃, the characteristic conformation of apoprotein consists of polypeptide chain of both subunits have been proved to be α helix and β turn, respectively, in various region. The aromatic side chains of both tyrosine and tryptophan residue are partial exposed to the protein molecule surface. The relation between structural properties of C PC and low ionic strength solvent environment have been discussed.
出处
《光散射学报》
1999年第4期325-329,共5页
The Journal of Light Scattering
基金
江苏省教委自然科学基金
江苏省重点开放实验室自然科学基金
关键词
C-藻蓝蛋白
拉曼光谱
脱辅蛋白
藻
藻胆蛋白
Phycobiliprotein
C Phycocyanin
Raman spectra
Cyanobacterium
Apoprotein
