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首页> 外文期刊>Biochemistry >Comparative structure analysis of tyrosine and valine residues in unprocessed silk fibroin (silk I) and in the processed silk fiber (silk II) from Bombyx mori using solid-state (13)C,(15)N, and (2)H NMR.
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Comparative structure analysis of tyrosine and valine residues in unprocessed silk fibroin (silk I) and in the processed silk fiber (silk II) from Bombyx mori using solid-state (13)C,(15)N, and (2)H NMR.

机译：使用固态（13）C，（15）N和（2）H NMR对来自Bombyx mori的未加工丝素蛋白（丝I）和加工丝纤维（丝II）中酪氨酸和缬氨酸残基的比较结构分析。

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摘要

The solid-state (13)C CP-MAS NMR spectra of biosynthetically labeled [(13)C(alpha)]Tyr, [(13)C(beta)]Tyr, and [(13)C(alpha)]Val silk fibroin samples of Bombyx mori, in silk I (the solid-state structure before spinning) and silk II (the solid-state structure after spinning) forms, have been examined to gain insight into the conformational preferences of the semicrystalline regions. To establish the relationship between the primary structure of B. mori silk fibroin and the "local" structure, the conformation-dependent (13)C chemical shift contour plots for Tyr C(alpha), Tyr C(beta), and Val C(alpha) carbons were generated from the atomic coordinates of high-resolution crystal structures of 40 proteins and their characteristic (13)C isotropic NMR chemical shifts. From comparison of the observed Tyr C(alpha) and Tyr C(beta) chemical shifts with those predicted by the contour plots, there is strong evidence in favor of an antiparallel beta-sheet structure of the Tyr residues in the silk fibroin fibers. On the other hand, Tyr residues take a random coil conformation in the fibroin film with a silk I form. The Val residues are likely to assume a structure similar to those of Tyr residues in silk fiber and film. Solid-state (2)H NMR measurements of [3,3-(2)H(2)]Tyr-labeled B. mori silk fibroin indicate that the local mobility of the backbone and the C(alpha)-C(beta) bond is essentially "static" in both silk I and silk II forms. The orientation-dependent (i.e., parallel and perpendicular to the magnetic field) solid-state (15)N NMR spectra of biosynthetically labeled [(15)N]Tyr and [(15)N]Val silk fibers reveal the presence of highly oriented semicrystalline regions.
机译：生物合成标记的[（13）Cα] Tyr，[（13CCβ] Tyr和[（13）Cα] Val丝的固态（13）C CP-MAS NMR光谱家蚕丝素I（纺丝前的固态结构）和丝绸II（纺丝后的固态结构）的纤维蛋白样品已经过检验，以了解半结晶区的构象偏好。要建立桑蚕丝素蛋白的一级结构与“局部”结构之间的关系，需要针对TyrCα，TyrCβ和Val C（13）构象的化学位移等高线图α）碳是由40种蛋白质的高分辨率晶体结构的原子坐标及其特征性（13）C各向同性NMR化学位移生成的。通过将观察到的TyrCα和TyrCβ化学位移与等高线图预测的化学位移进行比较，有力的证据表明，丝素蛋白纤维中Tyr残基具有反平行的β-折叠结构。另一方面，Tyr残基在丝素I形式的丝蛋白膜中呈无规卷曲构象。 Val残基可能具有类似于丝纤维和薄膜中Tyr残基的结构。 [3,3-（2）H（2）] Tyr标记的桑蚕丝素蛋白的固态（2）H NMR测量表明，骨架和Cα-Cβ的局部迁移性丝I和丝II形式的键本质上都是“静态”的。生物合成标记的[（15）N] Tyr和[（15）N] Val丝纤维的取向依赖性（即平行于磁场且垂直于磁场）固态（15）N NMR光谱揭示了高度取向的存在半结晶区。

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