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Introduction Molecular self-assembly has emerged as a powerful strategy in biomedical and pharmaceutical areas [ 1 ]. In particular, peptide self-assembly has been extensively investigated, to study protein folding, to
had a negative slope at high frequency and sIL-2Rα had negative slopes at medium and high frequency ( Table 3 ). Correlation coefficients ( R 2 ) were high with values close to 1.0. The negative activation enthalpy is associated with the protein-folding
. Davis-Searles , PR , Saunders , AJ , Erie , DA , Winzor , DJ , Pielak , GJ . Interpreting the effects of small uncharged solutes on protein folding equilibria . Annu Rev Biophys Biomol Struct 2001 30 : 271 10.1146/annurev.biophys.30