蛋白质二级结构的真空紫外圆二色性研究  

Vacuum Ultraviolet Clrcular Dichroism Studieson Secondary Structure of Proteins.

作　　者：林波海[1] 

机构地区：[1]中国科学院生物物理研究所

出　　处：《生物化学与生物物理进展》1994年第1期67-69,共3页Progress In Biochemistry and Biophysics

摘　　要：利用同步辐射真空紫外圆二色谱仪和特制的样品池，测定溶液中蛋白质的真空紫外圆二色谱，测定波长低至１７５ｎｍ，并应用一种新的计算法分析计算了蛋白质５种二级结构的含量，所得结果与用Ｘ射线衍射法测定的结果一致。讨论了获得好的真空紫外圆二色谱的几个重要因素。结果表明，真空紫外圆二色法是目前测定溶液中蛋白质二级结构的较好方法之一。acuum ultraviolet circular dichroism (VUV-CD) spectra of proteins in solution have beenmeasured using synchrotron radiation vacuumultraviolet circular dichroism spectrometer anda special cell. The measurement wavelength isdown to 175nm. A new calculation method hasbeen applied for calculating the content of fivekinds of secondary structures of proteins.Their results are coincident with that from X-ray diffraction method. In order to get goodVUV-CD spectra, several important factorshave been discussed. The experiments showthat so far, VUV-CD analysis is one of the fa-vorable method for secondary structure studiesof proteins.

关 键 词：真空 紫外圆二色谱 蛋白 二级结构 

分 类 号：Q6－33[生物学—生物物理学]