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Updated: Jul 12, 2026

Microfluidic Mixers for Studying Protein Folding
Published on: April 10, 2012
Strange kinetic phase in the extremely early folding process of beta-lactoglobulin
Yuji O Kamatari1, Hironori K Nakamura, Kazuo Kuwata
1Division of Prion Research, Center for Emerging Infectious Diseases, Gifu University, Gifu 501-1194, Japan.
Abstract:
A continuous-wave probed laser-induced temperature jump system was constructed and applied to monitor the changes in tryptophan fluorescence of the beta-lactoglobulin during its folding; the kinetic phases were traced from 300 ns to 10 ms after a temperature jump. Notably, an early phase with typical squeezed-exponential characteristics, [exp[-(kt)(beta)], beta>1.0], was observed around several tens of microseconds after the temperature jump, which is actually the earliest phase ever observed for beta-lactoglobulin. This process can be explained by conformational shift occurring within the unfolded ensemble (U-->U'), which is followed by the non-native intermediate (I) formation of this protein.
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