利用酪氨酸残基的共振瑞利散射研究溶液中蛋白质构象  

Study of Protein Conformation in Solution by Tyrosine Residues RRS Spectrum

作　　者：张源[1] 林哲绚[1] 李慧[1] 罗文鸿[1] 

机构地区：[1]汕头大学医学院中心实验室,广东汕头515041

出　　处：《光谱学与光谱分析》2006年第11期2089-2092,共4页Spectroscopy and Spectral Analysis

基　　金：国家自然科学基金(30271139);广东省自然科学基金(022124);2003年度教育部"优秀青年教师资助计划"项目(教人司2003-355号)资助

摘　　要：基于酪氨酸残基K带激发峰在较高浓度的蛋白质溶液中表现出特征散射峰,通过Δλ=0同步荧光扫描识别,建立用荧光分光光度法测定酪氨残基K带的共振散射峰强度及其波长位移来推测溶液中蛋白质构象变化的新方法。方法不受蛋白质色氨酸残基的干扰,图谱简单明了直观。文章叙述了方法建立的实验基础,并用构建的方法研究了盐效应、酸碱性效应对蛋白质构象变化的影响,最后通过测定不同温度下酶活性的实验验证了方法对温度影响酶蛋白质构象变化的分析的正确性。Due to the interference caused by the emission of tryptophan residue, it is hard to use fluorospectrophotometry to detect the spectrometric changes of the tyrosine residue when protein conformation is changed. When the concentration of protein in solution is relatively high, tyrosine residue has a characteristic scattering peak when excited with its K-band wavelength of light. In the present study, the authors established a method for detecting protein conformation changes in solution through the changes （peak height and wavelength shift） of the characteristic scattering peak of tyrosine residue. The method may be used for detecting protein conformation changes in solution caused by the changes of electrolyte, pH, and temperature.

关 键 词：蛋白质构象 酪氨酸残基 共振瑞利散射 

分 类 号：O657.3[理学—分析化学]