Precise Conformational Analysis of Some Polypeptides in the solution and liquid crystalline states by multi-nuclear NMR

利用多核核磁共振对溶液和液晶态中的某些多肽进行精确构象分析

• 批准号: 62470091
• 负责人: ANDO Isao
• 金额: $ 4.03万
• 依托单位: Tokyo Institute of Technology
• 依托单位国家: 日本
• 项目类别: Grant-in-Aid for General Scientific Research (B)
• 财政年份: 1987
• 资助国家: 日本
• 起止时间: 1987 至 1989
• 项目状态: 已结题
• 来源: https://kaken.nii.ac.jp/en/grant/KAKENHI-PROJECT-62470091/
• 关键词: polypeptide; protein; NMR; conformation; liquid crystal; サ-モトロピック液晶; 金属イオン輸送; イオノホア; 固体高分解能NMR; NMR化学シフト; コンホメーション; ヘリックス; 水素結合; 液晶; サーモトロピック液晶; 全属イオン輸送

We have demonstrated that solid state ^<13>C and ^<15>N NMR chemical shift values become fundamental data for analyzing conformation of polypeptides in the solid state, solution state and liquid crystalline state. Using the fundamental data, the origin of the formation and no formation of thermotropic liquid crystals for polypeptides with long akyl side chains has been clarified using variable temperature high resolution NMR spectroscopy. Further, higher-order structure of proteins in solution has been determined on the basis of solid state ^<13>C and ^<15>N NMR chemical shift values.The hydrogen bond plays an important role in forming the stable conformation of polypeptides and proteins. In order to investigate the effect of on the ^<13>C NMR chemical shifts of carbonyl carbons in peptides in the solid state, ^<13>C CP/ MAS NMR spectra were measured for a series of the oligopeptides containing glycine residues of which the crystal structures were already determined by X-ray diffraction We have found that the ^<13>C chemical shifts of the carbonyl carbon in the amide type hydrogen bond form move downfield with a decrease in the hydrogen bond length. This experimental finding is very useful to know the nature of hydrogen bond.The relationship between the conformation and the biochemical function in biologically-related compounds such as ionophores has been successfully studied by ^<13>C-NMR spectroscopy.

我们已经证明，固态~ <13>1C和~ 1 <15>N NMR化学位移值是分析多肽在固态、溶液态和液晶态构象的基础数据。使用的基本数据，形成和没有形成的热致液晶的多肽与长烷基侧链的起源已澄清使用变温高分辨率NMR光谱。根据固体~ 1C和~ 1 N NMR化学位移值确定了蛋白质在溶液中的高级结构<13><15>，氢键在形成多肽和蛋白质稳定构象中起着重要作用。为了研究<13>固态肽中羰基碳的~ 13 C NMR化学位移<13>的影响，测定了一系列已用X射线衍射确定晶体结构的甘氨酸残基寡肽的~ 13 C CP/ MAS NMR谱，发现<13>酰胺型氢键形式的羰基碳的~ 13 C化学位移随氢键长度的减小而向低场移动。这一实验结果对于认识氢键的本质是非常有用的。~ 13 C-NMR谱已成功地研究了生物相关化合物如离子载体的构象与生化功能之间的关系<13>。

项目成果

Shinji,Ando: J. Amer. Chem. Soc.110. 3380-3386 (1988)

安藤真嗣：J. Amer。

Shinji Ando: J.Amer.Chem.Soc.

安藤真司：J.Amer.Chem.Soc。

Kazuo Yamaguchi: Bull.Chem.Soc.Japan.

山口一夫：Bull.Chem.Soc.Japan。

Kazuo Yamaguchi: "Studies on synthetic ionophores VIII" Bull.Chem.Soc.Japan. 62. 1097-1101 (1989)

Kazuo Yamaguchi：“合成离子载体的研究 VIII”Bull.Chem.Soc.Japan。

B.Mohanty, T.Komoto, J.Watanabe, I.Ando and T.Shiibashi: "Conformation Aspect of Poly(gamma-oleyl L-glutamate) with Long Flexible Side Chains As Studied by Variable-Temperature ^<13>C CP/MAS NMR Spectroscopy" Macromolecules, 22, 4451-4455 (1989).

B.Mohanty、T.Komoto、J.Watanabe、I.Ando 和 T.Shiibashi：“通过可变温度 ^<13>C CP 研究具有长柔性侧链的聚（γ-油基 L-谷氨酸）的构象方面