Dilatometric and refractometric studies of the helix—coil transition of poly‐L‐glutamic acid in aqueous solution

The helix—coil transition of poly‐ L ‐glutamic acid (PGA) in aqueous solutions was followed by volume changes, Δ V , and also differential refractive indices, Δ n . The increase in Δ V or decrease in Δ n upon mixing the sodium salt of PGA with dilute HCl gave three straight lines between pH 7 and 4, the two breaks corresponding to the transition zone observed by other physical methods. For the reaction: COO − + H + → CO‐OH, Δ V per mole of H + bound was 11.4 and 11.1 ml. in 0.01 and 0.2 M NaCl solutions, respectively. An additional conformational change of about 0.5–1 ml. per amino acid residue was observed for the reaction: coil → helix, after taking electrostatic interaction into consideration. This was probably due to the release of the water of hydration at the amide linkages when the polypeptide coil is converted into the α‐helix, or even the occurrence of voids in the polypeptide chain as a result of imperfect packing of the atoms, although the origin of this volume change is still not fully understood at the present time. The volume changes as calculated from Δ n by assuming a constant polarizability of the polymer was found to be higher for the association reaction than those mentioned above. On the other hand, the calculated Δ V for the transition was in fair agreement with those by direct measurements.