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Trends for the experimental transitional voltages required for inducing unfolding for the stability of the FGF1–HS complexes in the 1:1 (a) and 2:1 (c) binding stoichiometry compared with the trends for theoretical binding free energies for the 1:1 (b) and 2:1 (d) complexes. The two trends are comparable, indicating that the binding of longer heparin oligosaccharides imparts greater stability to the protein against unfolding
