The optical and rotatory properties of poly-L-tyrosine (PLT) dissolved in trimethyl phosphate and in water have been measured.The results, however, cannot be explained in terms of one conformation or another, since the side-chains chromophores interact with the peptide groups or among themselves, thus giving rise to complex circular dichroic spectra.I R measurements carried out on films of PLT cast from trimethylphasphate (FMP) or directly on solutions of the polymer in TMP strongly suggest that the polypeptide assumes an a-helical conformation.The sense of spiralizaCon of the helix cannot be obtained with such measurements. ZUSAMMENFASSUNG:Es wurden die optischen und polarimetrischen Eigenschaften von Poly-L-tyrosin (PLT) in Trimethylphosphat und Wasser als Losungsmittel untersucht.Die Ergebnisse konnen jedoch nicht durch das Vorliegen einer bestimmten Konformation gedeutet werden, da Wechselwirkungen der Seitenketten-Chromophore mit sich selbst oder mit Peptidgruppen zu komplexen CD-Spektren fiihren.IR-Messungen an Filmen von PLT, die aus Trimethylphosphat (TMP) gegossen waren, oder direkt an Losungen des Polymeren in TMP machen wahrscheinlich, da13 das Polypeptid eine a-helikale Konformation ausbildet.Der Helixsinn kann aus solchen Messungen jedoch nicht bestimmt werden.
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