Stability of the folded-chain beta-structure of a homopolypeptide based on time-resolved potentiometric titrations.
The standard free energy change of the unimolecular conversion between the folded-chain beta-structure and random coil of uncharged poly(S-carboxymethyl-L-cysteine) was evaluated from the potentiometric titration curves extrapolated to zero time to reduce the effect of aggregation which occurred at slower rates than chain folding for most degrees of ionization. To reduce the remaining contribution from the aggregation, the results obtained at finite concentrations were further extrapolated to zero polymer concentration. A value of -(400 +/- 100) cal/mol was obtained for a sample of chain length 630. From the titration curves at the aggregation equilibrium, the total free energy change of the whole solution associated with the same conversion was determined. The contribution made by aggregation to the stability was determined from the difference between these two quantities, which turned out to be comparable with that from the unimolecular conversion.
Department of Chemistry, Faculty of Science, Nagoya University, Japan.
M
M
Kimura
H
H
Maeda
S
S
Ikeda
D004355:Drug Stability; D007700:Kinetics; D046911:Macromolecular Substances; D010455:Peptides; D011199:Potentiometry; D011487:Protein Conformation; D013997:Time Factors
D046911:Macromolecular Substances; D010455:Peptides; C036002:poly(S-carboxymethylcysteine)