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Article
Early Aggregated States in the Folding of Interleukin-1β
Journal of Biological Physics
  • John M. Finke, University of Washington Tacoma
  • P. A. Jennings
Publication Date
6-1-2001
Document Type
Article
Abstract

Kinetic data measured from folding of the protein interleukin-1β fits best to three exponential phases when studied with tryptophan fluorescence but only two exponential phases when measured using other methods. The technique of ANS fluorescence was used to determine whether the additional phase observed in tryptophan fluorescence was also detected with ANS dye binding. Unlike trytophan fluorescence, the ANS fluorescence was highly dependent on the concentration of protein present during the folding experiment. Experimental controls provide evidence that ANS binds to protein aggregates, present at higher concentrations and absent at lower concentrations. Protein concentration-dependent folding studies demonstrate that, at lower interleukin-1β concentrations, tryptophan fluorescence kinetics can be fit adequately with a two exponential fit. This study indicates that (1) measured interleukin-1β folding kinetics fit to a 2 phase model and (2) at higher protein concentrations, transient association of IL-1β may result in a kinetic fit of 3 phases.

DOI
10.1023/A:1013178505077
Version
pre-print, post-print
Citation Information
John M. Finke and P. A. Jennings. "Early Aggregated States in the Folding of Interleukin-1β" Journal of Biological Physics Vol. 27 Iss. 2 (2001) p. 119 - 131
Available at: http://works.bepress.com/john_finke/16/