Science Advances

Supplementary Materials

This PDF file includes:

  • Fig. S1. FLNC and HspB1 are up-regulated and partially colocalize in mechanically challenged mouse heart.
  • Fig. S2. Phosphorylation of HspB1 modulates the interaction with FLNCd18–21.
  • Fig. S3. Solution NMR of truncated HspB1 variants reveals changes in the dynamics of HspB1 ACD residues upon phosphomimicry.
  • Fig. S4. A crystal structure of the HspB1 ACD in complex with a peptide mimic of N-terminal residues reveals conformational heterogeneity of the PPR and β2 strand.
  • Fig. S5. (P)HspB180–88 binds FLNCd18–21 specifically with phosphorylation modifying the extension of the complex.
  • Fig. S6. Coulombically steered unfolding can prompt biologically relevant transitions within FLNC.
  • Fig. S7. Stabilization of an intermediate FLNC unfolding state by HspB1 phosphopeptide is observed across charge states and instrument conditions.
  • Table S1. Data collection and refinement statistics for HspB184–170 in complex with PPR peptide.
  • Table S2. Guide to nomenclature for recombinant proteins and synthetic peptides used in this study.

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