Physicochemical studies of a branched polypeptide antigen: poly(L-Tyr,L-Glu)-poly(DL-Ala)--poly(L-Lys).
The synthesis of a branched polypeptide, poly(L-Tyr,L-Glu)-poly(DL-Ala)--poly(L-Lys), is described. Physicochemical investigations of the polymer by means of hydrogen-deuterium exchange, potentiometric titrations, and viscosity measurements indicate a non-ordered, flexible conformation in aqueous solution, depending on pH and salt concentration. A hysteresis phenomenon observed in the titrations is tentatively ascribed to interactions between the sidechains, and in accordance with observations from the infrared spectrum of the polymer it is suggested that rather slow conformational changes of the polymer molecules occur in aqueous solutions. The immunochemical implications of the physiochemical findings are discussed with special reference to the concept of sequential and conformational determinants.
D000409:Alanine; D000941:Antigens; D003903:Deuterium; D000939:Epitopes; D005971:Glutamates; D006859:Hydrogen; D006863:Hydrogen-Ion Concentration; D007526:Isoelectric Point; D008239:Lysine; D010455:Peptides / Q000138:chemical synthesis / Q000276:immunology; D011487:Protein Conformation; D013055:Spectrophotometry, Infrared; D013329:Structure-Activity Relationship; D014443:Tyrosine; D014783:Viscosity
D000941:Antigens; D000939:Epitopes; D005971:Glutamates; D010455:Peptides; D014443:Tyrosine; D006859:Hydrogen; D003903:Deuterium; D008239:Lysine; D000409:Alanine