Following protein folding in real time using NMR spectroscopy


The refolding of apo bovine α-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… (More)
DOI: 10.1038/nsb1095-865