Transient non-native secondary structures during the refolding of α-lactalbumin detected by infrared spectroscopy
Transient non-native secondary structures during the refolding of α-lactalbumin detected by infrared spectroscopy
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红外光谱检测α-乳清蛋白重折叠过程中的瞬时非天然二级结构
DOI：
10.1038/71286
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发表时间：
2000
期刊：
影响因子：
--
通讯作者：
V. Forge
中科院分区：
文献类型：
--
作者：
A. Troullier;D. Reinstädler;Y. Dupont;D. Naumann;V. Forge
采用停流傅里叶变换红外光谱（SF-FTIR）对钙结合蛋白α-乳清蛋白复性过程中的天然和非天然二级结构进行了鉴定。红外吸收光谱记录在真实的时间后的pH跳跃诱导的蛋白质的重折叠。在钙存在下，重折叠快速，二级结构一致出现;在钙不存在下，折叠慢得多且复杂，非天然β-折叠短暂形成和消失。同时检测天然结构和非天然结构的可能性在深入了解蛋白质重折叠过程的复杂性方面特别有价值。
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.