Strange kinetic phase in the extremely early folding process of β-lactoglobulin

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A continuous-wave probed laser-induced temperature jump system was constructed and applied to monitor the changes in tryptophan fluorescence of the β-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)β}, β > 1.0], was observed around several tens of microseconds after the temperature jump, which is actually the earliest phase ever observed for β-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. © 2007 Federation of European Biochemical Societies.




Kamatari, Y. O., Nakamura, H. K., & Kuwata, K. (2007). Strange kinetic phase in the extremely early folding process of β-lactoglobulin. FEBS Letters, 581(23), 4463–4467.

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