A 2H NMR study of (Ser-3,3-2H2)- and (Ala-3,3,3-2H3)- silk fibroins in the solid state. Role of side-chain moiety in stabilization of secondary structure.
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概要
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An attempt was made to prepare [<I>Ser</I>-3,3-<SUP>2</SUP>H<SUB>2</SUB>]- and [<I>Ala</I>-3,3,3-<SUP>2</SUP>H<SUB>3</SUB>]-fibroins by feeding respective amino acids DL-[3,3-<SUP>2</SUP>H<SUB>2</SUB>]-serine (Ser) and [3,3,3-<SUP>2</SUP>H<SUB>3</SUB>]-alanine (Ala), respectively, to silkworms, <I>Bombyx mori</I> and <I>Philosamia cynthia ricini</I> together with daily artificial diet. We recorded <SUP>2</SUP>H powder-pattern NMR spectra of [<I>Ser</I>-3,3-<SUP>2</SUP>H<SUB>2</SUB>]- and [<I>Ala</I>-3,3,3-<SUP>2</SUP>H<SUB>3</SUB>]-cocoons and fibroins (10–20% deuteration) by means of the quadrupole echo method. It was found that separation of the <SUP>2</SUP>H quadrupole splittings is 125 and 39 kHz, respectively, for [<I>Ser</I>-3,3-<SUP>2</SUP>H<SUB>2</SUB>]- and [<I>Ala</I>-3,3,3-<SUP>2</SUP>H<SUB>3</SUB>]-cocoons and fibroins, respectively. Accordingly, it was concluded that side-cain reorientation of Ser residue is virtually frozen irrespective of differences in conformations of silk I and silk II, suggesting that the hydroxyl groups in these cases might be hydrogen-bonded to C=O or NH groups in intra or interchain. On the other hand, side-chain methyl group of Ala residue in [<I>Ala</I>-3,3,3-<SUP>2</SUP>H<SUB>3</SUB>]-fibroin turned out to undergo rapid three-fold rotation about the C<SUB>α</SUB>–C<SUB>β</SUB> axis, as viewed from data of the quadrupole splittings.
- 公益社団法人 日本化学会の論文
著者
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Asakura Tetsuo
Department Of Biochemistry And Life Sciences Faculty Of Technology Tokyo University Of Agriculture A
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Saito Hazime
Biophysics Division, National Cancer Center Research Institute
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Tabeta Ryoko
Biophysics Division
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Kuzuhara Akio
Department of Polymer Engineering, Tokyo University of Agriculture and Technology
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