Concentration Dependence of the Conversion between the Intermolecular β-Structure and the Disordered State of Poly(S-carboxymethyl-l-cysteine) in Aqueous Solutions
- 1 February 1983
- journal article
- research article
- Published by Oxford University Press (OUP) in Bulletin of the Chemical Society of Japan
- Vol. 56 (2) , 602-606
- https://doi.org/10.1246/bcsj.56.602
Abstract
The effects of polymer concentration on the reversible conversion between the intermolecular β-structure and the disordered state of poly(S-carboxymethyl-L-cysteine) were examined by means of circular dichroism at constant pHs in 20 mM NaClO4 solutions. The data were tentatively analyzed based on an assumed all-or-none model. A value of −1.1 kJ (−250 cal) per mole of residues was obtained for the standard free energy of association. It was suggested that the obtained results depended significantly on the molecular weight distribution of the used samples.Keywords
This publication has 10 references indexed in Scilit:
- .beta.-Structure of poly[S-(carboxymethyl)-L-cysteine] in aqueous solutions by intermolecular association and intramolecular chain foldingMacromolecules, 1982
- Isodichroic point and the β–random coil transition of poly(S‐carboxymethyl‐L‐cysteine) and poly(S‐carboxyethyl‐L‐cysteine) in the absence of added saltBiopolymers, 1981
- Circular dichroism and the pH‐induced β‐coil transition of poly(S‐carboxymethyl‐L‐cysteine) and its side‐chain homologBiopolymers, 1979
- Thermodynamic Parameters for the Intramolecular Disordered-to-β Transition of Poly(Ltyrosine) in Aqueous SolutionMacromolecules, 1976
- Potentiometric titrations involving the β‐coil transitionBiopolymers, 1975
- Conformational states of poly(L‐tyrosine) in aqueous solutionBiopolymers, 1975
- Potentiometric titration of poly‐L‐lysine: the coil‐to‐β transitionBiopolymers, 1971
- Circular dichroism of .beta.-poly-L-lysineJournal of the American Chemical Society, 1969
- Two Rippled-Sheet Configurations of Polypeptide Chains, and a Note about the Pleated SheetsProceedings of the National Academy of Sciences, 1953
- Configurations of Polypeptide Chains With Favored Orientations Around Single BondsProceedings of the National Academy of Sciences, 1951