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

[1]

Levinthal C., Are there pathways for protein folding?, J. Chim. Phys, 65, pp. 44-45, (1968)

[2]

Plaxco K.W., Dobson C.M., Time-resolved biophysical methods in the study of protein folding, Curr. Opin. Struct. Biol., 6, pp. 630-636, (1996)

[3]

Van Nuland N.A.J., Forge V., Balbach J., Dobson C.M., Real-time NMR studies of protein folding, Acc. Chem. Res., 31, pp. 773-778, (1998)

[4]

Englander S.W., Mayne L., Protein folding studied using hydrogen-exchange labeling and two dimensional NMR, Annu. Rev. Biophys. Biomol. Struct., 21, pp. 243-265, (1992)

[5]

Ptitsyn O.B., Structures of folding intermediates, Curr. Opin. Struct. Biol., 5, pp. 74-78, (1995)

[6]

Shortle D.R., Structural analysis of non-native states of proteins by NMR, Curr. Opin. Struct. Biol., 6, pp. 24-30, (1996)

[7]

Dyson H.J., Wright P.E., Equilibrium NMR studies of unfolded and partially folded proteins, Nature Struct. Biol., 5, SUPPL., pp. 499-503, (1998)

[8]

Dill K.A., Chan H.S., From Levinthal to pathways to funnels, Nature Struct. Biol., 4, pp. 10-19, (1997)

[9]

Dobson C.M., Sali A., Karplus M., Protein folding: A perspective from theory and experiment, Angew. Chem. Int. Ed., 37, pp. 868-893, (1998)

[10]

Shiraki K., Nishikawa K., Goto Y., Trifluoroethanol-induced stabilization of the α-helical structure of β-lactoglobulin: Implication for non-hierarchical protein folding, J. Mol. Biol., 245, pp. 180-194, (1995)

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