Publisher Summary This chapter focuses on the capacity of the optical rotatory methods to discern mixtures of this conformation with disordered regions. It discusses the manner in which theoretical considerations have provided the forms into which rotatory data are currently cast, the calibration of their constants by studies of synthetic polypeptides in known conformation, and then, the application of these equations and scales in the structural interpretation of the rotatory dispersion of proteins. This pattern of analysis undergoes refinement and revision as these methods are applied to new species of polypeptide and protein in concert with other means of conformational assignment. An extension of the spectral range of measurement toward optically active absorption bands in the far ultraviolet is expected to yield new information about the rotatory power of the peptide bond and thus enhance the interaction of theory and observation that has already proved fruitful.

Optical rotation and the conformation of polypeptides and proteins.

Chapter 6 – Intramolecular Bonds in Proteins. II. Noncovalent Bonds

The synthesis of casein-g-poly(methyl acrylate) was studied using the potassium peroxydisulfate–ascorbic acid redox system. The effect of synthetic variables has been investigated in the light of rates of conversion of monomer, graft copolymerization and homopolymerization, percent grafting, and grafting efficiency. The results are compared with the system initiated by pure potassium peroxydisulfate alone.

Synthesis of casein‐g‐poly(methyl acrylate). II

The sharpness of the transition in reversible protein denaturation1

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The sharpness of the transition in reversible protein denaturation1