Nuclear magnetic resonance study on the relationship between the helicity and L-alanine content of L-alanine/β-alanine random copolypeptides in connection with silk fibroin conformation

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Description

he helicities of six kinds of L-alanine/β-alanine random copolypeptides having different L-alanine contents were determined using ^1H NMR. Next, the theoretical helicities of these copolypeptides were calculated on the basis of a statistical thermodynamic analysis of the helixcoil transition of the random copolypeptide -using Monte Carlo methods- as a function of the L-alanine content. The statistical weight parameters used in the model were determined from a comparison of the observed and calculated results. The experimental and theoretical results are in agreement with the fact that Bombyx mori silk fibroin with 30,0 mo1-% L-alanine content assumes exclusively a random-coil conformation and that philosamia cynthia ricini silk fibroin with 48,8 mol-% L-alanine content locally assumes an α-helical conformation in the sequence of the L-alanine residues, both in aqueous solution.

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Details 詳細情報について

  • CRID
    1570291226923447040
  • NII Article ID
    110001072263
  • NII Book ID
    AN10371516
  • ISSN
    09129545
  • Text Lang
    en
  • Data Source
    • CiNii Articles

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