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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概要

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• 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.

• 関西鍼灸大学の論文
• 1990-04-01

著者

• Kashiba Hitoshi

  Kansai College Of Acupuncture Medicine

• Asakura Tetsuo

  Faculty of Technology, Tokyo University of Agriculture and Technology

• Komoto Tadashi

  Faculty of Technology, Gunma University

• Komoto Tadashi

  Faculty Of Technology Gunma University

• Asakura Tetsuo

  Faculty Of Technology Tokyo University Of Agriculture And Technology

関連論文

• 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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