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Journal/Book: J Am Chem Soc
Published: 2000
Pages: 6169 - 6174
Volume: 122
Issue: 26
Accession no.: 41
ISBN: 0002-7863

Monitoring the Kinetics of Ion-Dependent Protein Folding by Time-Resolved NMR Spectroscopy at Atomic Resolution

Kühn, Till, Harald Schwalbe
The kinetics of protein refolding have been monitored by time-resolved NMR spectroscopy. It is shown that refolding of metal binding proteins can be induced by photolysis of photo labile ion chelators, the subsequent release of Ca2+ ions can induce protein folding, and the changes in resonance positions can be monitored by time-resolved NMR spectroscopy. The feasibility of the approach is demonstrated by characterizing the refolding of α-lactalbumin, or protein containing a Ca2+ binding site, unfolded in 4 M urea at pH 7 in the absence of Ca2+. The refolding kinetics of the methyl groups of residues Leu15 and Val21 in the core of the protein have been determined to be mono-exponential with rates of 0.28 s-1 and 0.23 s-1, respectively at 300 K.
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Prof. Dr. Harald Schwalbe
Institut für Organische Chemie und Chemische Biologie
Johann Wolfgang Goethe Universität
Max-von-Laue-Str. 7
D-60438 Frankfurt am Main
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