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Supplementary Materials

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  • fig. S1. Unprocessed SPR traces for the data in Fig. 2A showing the binding trace for the experimental flow cell (black) and the control flow cell (red).
  • fig. S2. Point mutations to both SH2 domains of SHP-1 result in minimal binding but appreciable dephosphorylation.
  • fig. S3. Comparison of the standard and MPDPDE model fits.
  • fig. S4. Theoretical SPR traces generated by the MPDPDE model.
  • fig. S5. MCMC analysis of the experimental data in Fig. 2A highlights that all five parameters can be determined independently of each other.
  • fig. S6. Quality control of experimental data.
  • fig. S7. Surface tethering markedly increases the rate of dephosphorylation.
  • fig. S8. Calculation of local concentration, σ(r), based on two polymers a distance of r apart that can be approximated by worm-like chains with parameter LA for the free phosphorylated peptide and LB for the SHP-1–bound phosphorylated peptide.

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