Optical rotation and helical polypeptide chain configuration in collagen and gelatin.

The optical rotation phenomena exhibited by a citrate-extracted fraction of ichthyocol (from carp swim bladder), as well as by the parent gelatin derived therefrom, have been studied. Dispersion data for all cases follow a single-term Drude equation, but the variations with state are adequately expressed by simple reference to changes in alpha as follows:- 1. The native collagen fraction, dispersed in 0.15 M citrate buffer at pH 3.7 in the cold (11 degrees C.), yields a high negative specific rotation, alpha, near -350 degrees . 2. During equilibration at 40 degrees C., which causes conversion to a monodisperse parent gelatin, the rotation drops to about -110 degrees . 3. Gelation at 2 degrees C. results in a partial regain of rotation to around -290 degrees . This mutarotation is reversible, depending on temperature. 4. In the range 0.02 to 0.28 per cent the native ichthyocol and the warm gelatin solutions show little concentration dependence, but with the cold gelatin solutions the specific rotation increases with concentration. Gelatin films formed by cold evaporation yield high specific rotation (ca. -620 degrees ), but those formed by hot evaporation retain low optical activity. 5. Since this same collagen-gelatin system has been investigated physicochemically, it is possible to relate molecular changes to the observed variations in optical rotation. Conclusions are similar to those of Robinson (1953), who studied other gelatins: high negative rotation is believed related to a native collagen polypeptide configuration, herein specified as helical (from x-ray diffraction considerations) and destroyed by heating. The possible roles of intermolecular interactions and of prevalent pyrrolidine constituents in influencing the helical configuration and optical activity are discussed.