Following protein folding in real time using NMR spectroscopy.

TitleFollowing protein folding in real time using NMR spectroscopy.
Publication TypeJournal Article
Year of Publication1995
AuthorsBalbach, J., V. Forge, N. A. J. van Nuland, S. L. Winder, P. J. Hore, and C. M. Dobson
JournalNat Struct Biol
Date Published1995 Oct
KeywordsCircular Dichroism, Lactalbumin, Magnetic Resonance Spectroscopy, Models, Molecular, Protein Denaturation, Protein Folding, Time Factors

The refolding of apo bovine alpha-lactalbumin has been monitored in real time by NMR spectroscopy following rapid in situ dilution of a chemically denatured state. By examining individual resonances in the time-resolved NMR spectra, the native state has been shown to emerge in a cooperative manner from an intermediate formed in the dead-time of the experiments. The kinetics of folding to the native state are closely similar to those observed by stopped-flow fluorescence and near-UV circular dichroism. The NMR spectrum of the transient intermediate resembles closely that of the well characterized stable molten globule state formed at low pH. The results suggest that NMR can play a key role in describing at an atomic level the structural transitions occurring during protein folding.

Alternate JournalNat. Struct. Biol.
PubMed ID7552710