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Conformational studies on copolymers of L ‐leusine and L ‐leucine: Circular dichroism and potentiometric titration studies
Author(s) -
Snell Christopher R.,
Fasman Gerald D.
Publication year - 1972
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1972.360110817
Subject(s) - chemistry , potentiometric titration , circular dichroism , titration curve , copolymer , titration , monomer , leucine , mole fraction , residue (chemistry) , crystallography , mole , amide , polymer , analytical chemistry (journal) , stereochemistry , amino acid , chromatography , organic chemistry , biochemistry , electrode
Conformational aspects of a series of copolymers of L ‐Leucine and L ‐leucine [poly‐(Lys x Leu y )] containing 0 to 0.41 mole fraction L ‐leucine have been studied by circular dichroism (CD) and potentiometric titration in 0.05 M KF solution. CD studies on the α‐helical conformation showed a dependence of the magnitude of the CD ellipticity band at 222 nm on copolymer composition; the [θ] 222 decreasing with higher leucine contents. This was interpreted as the result of an increase of the hydrophobicity of the environment of the amide group due to the presence of the leucyl residues. Values of the Zimm‐Rice parameter, σ, for the copolymers were obtained from the potentiometric titrations and used to fit theoretical curves to the experimental data. Using the variation of σ with polymer composition, a value of σ for the leucyl residue was estimated to be 6.3 × 10 −2 , assuming independence of σ on the amino acid sequence in the copolymer. The free energy change for the conversion of one mole residue from uncharged helix to uncharged coil, Δ G hc °, was also obtained from the titration data for each copolymer up to a leucine mole fraction of 0.16; a value of 385 cal mole −1 was estimated for Δ G hc ° for a leucyl residue. These values for σ and Δ G hc ° are compared with other values in the literature for various amino acid residues obtained from titration and melting curve data.