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Updated: Jul 31, 2026

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
Published on: June 27, 2014
Transient non-native secondary structures during the refolding of alpha-lactalbumin detected by infrared spectroscopy
A Troullier1, D Reinstädler, Y Dupont
1Laboratoire de Biophysique Moléculaire et Cellulaire, URA CNRS 520, Département de Biologie Moléculaire et Structurale, CEA-Grenoble, 17 av. des Martyrs, 38054 GRENOBLE Cedex 09, France.
Abstract:
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 alpha-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 beta-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.
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