| Abstract
| - The kinetics of protein refolding have been monitored by time-resolved NMR spectroscopy. It isshown that refolding of metal binding proteins can be induced by photolysis of photo labile ion chelators, thesubsequent release of Ca2+ ions can induce protein folding, and the changes in resonance positions can bemonitored by time-resolved NMR spectroscopy. The feasibility of the approach is demonstrated by characterizingthe refolding of α-lactalbumin, or protein containing a Ca2+ binding site, unfolded in 4 M urea at pH 7 in theabsence of Ca2+. The refolding kinetics of the methyl groups of residues Leu15 and Val21 in the core of theprotein have been determined to be mono-exponential with rates of 0.28 s-1 and 0.23 s-1, respectively at300 K.
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