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首页> 外文期刊>Journal of the American Chemical Society >Structural Analysis of Alanine Tripeptide with Antiparallel and Parallel beta-Sheet Structures in Relation to the Analysis of Mixed beta-Sheet Structures in Samia cynthia ricini Silk Protein Fiber Using Solid-State NMR Spectroscopy
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Structural Analysis of Alanine Tripeptide with Antiparallel and Parallel beta-Sheet Structures in Relation to the Analysis of Mixed beta-Sheet Structures in Samia cynthia ricini Silk Protein Fiber Using Solid-State NMR Spectroscopy

机译：使用固态NMR光谱分析平行和平行的β-Sheet结构的丙氨酸三肽与Samia cynthia ricini丝蛋白纤维中混合的beta-Sheet结构的关系

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摘要

The structural analysis of natural protein fibers with mixed parallel and antiparallel beta-sheet structures by solid-state NMR is reported.To obtain NMR parameters that can characterize these beta-sheet structures,~(13)C solid-state NMR experiments were performed on two alanine tripeptide samples:one with 100% parallel beta-sheet structure and the other with 100% antiparallel beta-sheet structure.All ~(13)C resonances of the tripeptides could be assigned by a comparison of the methyl ~(13)C resonances of Ala_3 with different [3-~(13)C]Ala labeling schemes and also by a series of RFDR (radio frequency driven recoupling) spectra observed by changing mixing times.Two ~(13)C resonances observed for each Ala residue could be assigned to two nonequivalent molecules per unit cell.Differences in the ~(13)C chemical shifts and ~(13)C spin-lattice relaxation times (T_1) were observed between the two beta-sheet structures.Especially,about 3 times longer T_1 values were obtained for parallel beta-sheet structure as compared to those of antiparallel beta-sheet structure,which could be explicable by the difference in the hydrogen-bond networks of both structures.This very large difference in Ti becomes a good measure to differentiate between parallel or antiparallel beta-sheet structures.These differences in the NMR parameters found for the tripeptides may be applied to assign the parallel and antiparallel beta-sheet ~(13)C resonances in the asymmetric and broad methyl spectra of [3-~(13)C]-Ala silk protein fiber of a wild silkworm,Samia cynthia ricini.
机译：报道了通过固相NMR对具有平行和反平行β-折叠结构的天然蛋白纤维进行结构分析。为了获得可表征这些β-折叠结构的NMR参数，在〜（13）C固态NMR上进行了实验。两个丙氨酸三肽样品：一个具有100％平行β-折叠结构，另一个具有100％反平行β-折叠结构。三肽的所有〜（13）C共振可通过比较甲基〜（13）C来确定不同的[3-〜（13）C] Ala标记方案对Ala_3的共振，以及通过改变混合时间观察到的一系列RFDR（射频驱动再耦合）光谱。每个Ala残基可观察到两个〜（13）C共振被分配给每个单位细胞两个不等价的分子。在两个β-折叠结构之间观察到〜（13）C化学位移和〜（13）C自旋晶格弛豫时间（T_1）的差异。特别是长约3倍平行Beta获得T_1值与反平行β-折叠结构相比，这可以通过两个结构的氢键网络的差异来解释。Ti的这种巨大差异成为区分平行或反平行β-折叠的好方法三肽的NMR参数差异可用于在[3-〜（13）C] -Ala丝的不对称和宽甲基光谱中分配平行和反平行的β-sheet〜（13）C共振野生蚕的蛋白质纤维，Samia cynthia ricini。

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  • 来源
    《Journal of the American Chemical Society》 |2006年第18期|p.6231-6238|共8页
  • 作者

    Tetsuo Asakura; Michi Okonogi; Yasumoto Nakazawa; Kazuo Yamauchi;

  • 作者单位

    Contribution from the Department of Biotechnology,Tokyo University of Agriculture and Technology,2-24-16 Nakacho,Koganei,Tokyo 184-8588,Japan;

    Contribution from the Department of Biotechnology,Tokyo University of Agriculture and Technology,2-24-16 Nakacho,Koganei,Tokyo 184-8588,Japan;

    Contribution from the Department of Biotechnology,Tokyo University of Agriculture and Technology,2-24-16 Nakacho,Koganei,Tokyo 184-8588,Japan;

    Contribution from the Department of Biotechnology,Tokyo University of Agriculture and Technology,2-24-16 Nakacho,Koganei,Tokyo 184-8588,Japan;

  • 收录信息 美国《科学引文索引》(SCI);美国《工程索引》(EI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
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  • 正文语种 eng
  • 中图分类 化学;
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