Mendieta J, Folqué H, Tauler R
Departament de Química Analítica, Universitat de Barcelona, 08028-Barcelona,
Biophys J. 1999 Jan;76(1 Pt 1):451-7. doi: 10.1016/S0006-3495(99)77212-7.
The trifluoroethanol-dependent induction of the nonnative alpha-helical form of beta-lactoglubulin has been studied by circular dichroism spectroscopy. Data analysis is performed by factor analysis and multivariate curve resolution. An intermediate form in the induction of the alpha-helical form of the beta-lactoglobulin has been identified at low TFE concentration. By application of an alternating least-squares algorithm, the CD spectrum corresponding to the intermediate form has been resolved. The deconvolution of this CD spectrum shows a secondary structure content more in agreement with the one predicted from the amino acid sequence than the secondary structure of the helical form obtained at higher TFE concentrations. The additional alpha-helical content of the form present at higher TFE concentrations could be due to nonspecific interaction of TFE with the polypeptide chain.
通过圆二色光谱法研究了三氟乙醇依赖性诱导β-乳球蛋白非天然α-螺旋形式的过程。数据分析采用因子分析和多元曲线分辨法。在低三氟乙醇浓度下，已鉴定出β-乳球蛋白α-螺旋形式诱导过程中的一种中间形式。通过应用交替最小二乘法，解析出了对应于中间形式的圆二色光谱。该圆二色光谱的去卷积显示，其二级结构含量与根据氨基酸序列预测的二级结构更为一致，而非在较高三氟乙醇浓度下获得的螺旋形式的二级结构。在较高三氟乙醇浓度下存在的形式中额外的α-螺旋含量可能是由于三氟乙醇与多肽链的非特异性相互作用所致。
