DETERMINATION OF THE STRUCTURE OF [1-C-13]GLYCINE-[N-15]ALANINE DOUBLE-LABELED BOMBYX-MORI SILK FIBROIN FIBERS USING SOLID-STATE N-15 NMR

被引：20

作者：

ASAKURA, T ^{[1
]}

DEMURA, M ^{[1
]}

HIRAISHI, Y ^{[1
]}

OGAWA, K ^{[1
]}

UYAMA, A ^{[1
]}

机构：

[1] KATAKURA IND CO LTD, BIOL SCI RES INST, NAGANO 390, JAPAN

来源：

CHEMISTRY LETTERS | 1994年 / 12期

关键词：

D O I：

10.1246/cl.1994.2249

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

The C-13-N-15 dipolar splitting was observed for the oriented [1-C-13]glycine-[N-15]alanine Bombyx mori silk fibroin rods placed parallel to the magnetic field with N-15 solid state NMR spectroscopy. The isotope labeled and oriented silk fibroin samples were prepared by the cultivation of the middle silkgland from the silkworm. The angle between the C-13-N-15 peptide bond of the glycine-alanine sequence and the oriented axis was determined as 141 degrees from the coupling constant.

引用

页码：2249 / 2252

页数：4

共 12 条

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