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

页码：78 / 86

页数：8

共 55 条

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