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- W2054366986 abstract "The folding of randomly coiled poly(L-glutamic acid) to the helical state has been studied in N-methylacetamide by titration methods. Since this solvent would be expected to form amide-peptide group hydrogen bonds with the unfolded form of the polymer, to a first approximation no helix stabilization could come from intrapolymer hydrogen bonds. The titration data, collected from 30 to 70°C yield the following values per residue for the thermodynamic parameters governing the coil-helix reaction for the uncharged polymer: ΔG30°C°, −1. 9 ± 0.1 kcal; Δ H°, 0 ± 0.1 kcal; ΔS30°C°, 6.3 ± 0.6 eu. In N-methyl acetamide, the helix is an order of magnitude more stable than in water, and this stabilization appears to be entirely the result of the entropy gained by solvent molecules which are released from the polymer upon folding." @default.
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- W2054366986 date "1969-10-01" @default.
- W2054366986 modified "2023-09-25" @default.
- W2054366986 title "Helix-coil transition of poly(L-glutamic acid) inN-methylacetamide" @default.
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- W2054366986 doi "https://doi.org/10.1002/bip.1969.360080402" @default.
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