Transient non-native secondary structures during the refolding of α- lactalbumin detected by infrared spectroscopy

被引：106
|
作者：
Troullier A. [1 ]
Reinstädler D. [2 ]
Dupont Y. [1 ]
Naumann D. [2 ]
Forge V. [1 ]
机构：
[1] Lab. de Biophysique Molec. et Cell., URA CNRS 520, CEA-Grenoble, 38054 Grenoble Cedex 09
[2] Robert Koch-Institut, D-13353 Berlin
来源：
Nature Structural Biology | 2000年 / 7卷 / 1期
关键词：
D O I：
10.1038/71286
中图分类号：
学科分类号：
摘要：
Stopped-flow Fourier-transform infrared spectroscopy (SF-FTIR) was used to identify native as well as non-native secondary structures during the refolding of the calcium-binding protein α-lactalbumin. Infrared absorbance spectra were recorded in real time after a pH jump induced refolding of the protein. In the presence of calcium, the refolding is fast with concerted appearance of secondary structures; in its absence, folding is much slower and intricate, with transient formation and disappearance of non-native β- sheet. The possibility of detecting native as well as non-native structures at the same time is especially valuable in providing insight into the complexity of the refolding process of a protein.
引用
收藏
页码：78 / 86
页数：8
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