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     Quick Explanation


    Ionic-strength–linked amyloid fibril stability (from raw depolymerization thermodynamics)
    Using Thermodynamics of amyloid fibril formation from chemical depolymerization, we visualize (i) denaturant/ionic-strength thermodynamic parameters via DG⁰ and (ii) ionic-strength dependence via reported linearized relationships for glucagon and PI3K-SH3 fibrils.



     Long Explanation


    Ionic-strength linked amyloid fibril stability (raw depolymerization thermodynamics)
    We visualize what the paper reports directly: (1) DG⁰ values from depolymerization at different monomer concentrations and (2) ionic-strength dependence summarized as linearized parameters for log K vs √I for glucagon vs PI3K-SH3 fibrils, plus (3) the cooperative-model nucleation size n that best fits.

    Figure A β€” Depolymerization DG⁰ (thermodynamics)

    What this shows (grounded in the paper)
    • For glucagon fibrils, the paper reports DG⁰ values of βˆ’36.7, βˆ’38.8, βˆ’42.2 kJ/mol at three glucagon concentrations (reported as a set of depolymerization DG⁰ data points used in fits).
    • For PI3K-SH3 fibrils, the paper reports DG⁰ values of βˆ’64.7 and βˆ’71.1 kJ/mol at two PI3K-SH3 concentrations.
    Note: DG⁰ here is tied to the paper’s depolymerization model/fit procedure and sign convention; interpret comparisons within the paper’s framework, not as universal β€œstability” units.

    Figure B β€” Ionic-strength dependence (log K vs √I)

    Grounded comparison
    • The paper reports ionic-strength fit parameters for PI3K-SH3 as slope β‰ˆ 37.5 and intercept β‰ˆ 16.8 (from Fig. 4c extraction).
    • The paper reports ionic-strength fit parameters for glucagon as slope β‰ˆ 12.84 and intercept β‰ˆ 12.88 (from Fig. 4d extraction).
    Caution: these are fit-parameter summaries (not raw measurements across a continuous ionic strength grid provided here). The slope magnitude indicates how strongly the fitted model’s K responds to √I within the paper’s linearization.

    Figure C β€” Cooperative-model nucleation size (n)

    Evidence for the n range
    • The paper reports cooperative-model fits for nucleus sizes n and states best fits occur for n in the range 2–5 (with s β‰ͺ 1 also noted as part of the best-fit cooperative parameterization).

    How to read β€œionic strength stability” here

    Known vs uncertain (skeptical)
    • Known from the paper: PI3K-SH3 is more salt-sensitive than glucagon in the fitted ionic-strength dependence (larger reported slope for PI3K-SH3 than for glucagon).
    • Known from the paper: Cooperative polymerization (with nucleation/elongation parameters) describes depolymerization data more consistently than an isodesmic model across the explored protein concentration conditions in the studied systems.
    • Uncertain / not directly visualized from the provided raw extracts: The precise numeric mapping between √I values and experimental ionic strength (I units) and the full functional curve across all tested ionic strengths are not included in your provided extracted dataset; we therefore visualize only the reported linearized fit parameters and DG⁰ points.


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    Updated: April 22, 2026

     Top Data Sources ExportMCP


     Analysis Wizard



    It ingests the extracted DG⁰ points and ionic-strength fit slopes/intercepts from the provided paper data and generates publication-style summary plots for direct visual comparison between glucagon and PI3K-SH3.



     Hypothesis Graveyard


    A β€œpure isodesmic” mechanism would predict a single-constant description across protein concentrations with no need for separate nucleation/elongation parameters; but the paper reports cooperative fits yield more consistent DG⁰ behavior than isodesmic.


    An alternative β€œionic strength has no differential effect between fibril types” explanation is disfavored because the paper reports substantially different ionic-strength slopes (PI3K-SH3 slope ~37.5 vs glucagon ~12.84) in the same linearized framework.

     Science Art


    Visualize Data: Plot ionic strength stability amyloid PI3K-SH3 glucagon 10.1039/c9cp04524d Science Art

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