^<13>CNMRによるエリ蚕絹フィブロインならびにそのモデル化合物,アラニン,β-アラニンコポリマーの構造解析

概要

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The structures of Philosamia cynthia ricini silk fibroin and its model compounds, L-alanine/β-alanine copolymers, were studied in organic solvents, dichloroacetic acid (DCA) or trifluoroacetic acid (TFA) by means of ^<13>C NMR spectroscopy. In DCA, the carbonyl region of a series of L-alanine/β-alanine copolymers is divided into three peaks, corresponding to β-alanine (random coil), L-alanine (d-helix and random coil). 0n the other hand, the carbonyl region is more complex in TFA, indicating further splitting due to the primary structure in the coil state. Using the chemical shift data for the d-helix and random coil forms of the L-alanine residues of these copolymers in both solvents and statistical thermodynamic analysis for helix-coil transition, the spectra of the alanine carbonyl region of P. c. ricini silk fibroin in these solvents could be theoretically interpreted. Especially, the Lifson-Roig parameters in the thermodynamic treatment and the local helicity of each alanine residue of the -(Ala)_<22> - sequence were determined.
関西鍼灸大学の論文
1990-04-01