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. Author manuscript; available in PMC: 2012 Jul 18.
Published in final edited form as: Methods Enzymol. 2012;511:111–130. doi: 10.1016/B978-0-12-396546-2.00005-X

Figure 2.

Figure 2

Self-splicing constructs. A, Denaturing gel showing splicing products for a group II intron: (from top to bottom) lariat intron, unspliced precursor, linear intron, and spliced exons. B, Simulated plot of a splicing reaction showing the fraction of precursor as a function of time. The simulated data are fit by a single exponential curve to obtain rate constants for splicing in the presence (circles) and absence (diamonds) of protein. C, Simulated plot showing how the observed splicing rate varies with protein concentration. The rising linear portion of the data (circles) is fit with a line to obtain a second order rate constant for chaperone-accelerated folding. The plateau and decrease in rate (diamonds in gray area) reflect inhibition by the chaperone at higher concentrations (see section 3.1).