Solid state 19F NMR parameters of fluorine-labeled amino acids.: Part I:: Aromatic substituents
Solid state 19F NMR parameters of fluorine-labeled amino acids.: Part I:: Aromatic substituents
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氟标记氨基酸的固态 19F NMR 参数： 第一部分：：芳香族取代基
DOI：
10.1016/j.jmr.2007.11.017
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发表时间：
2008-03-01
影响因子：
2.2
通讯作者：
Ulrich, Anne S.
中科院分区：
文献类型：
--
作者：
Duerr, Ulrich H. N.;Grage, Stephan L.;Ulrich, Anne S.
生物膜中多肽和蛋白质的结构参数可以通过选择性标记氨基酸的固态核磁共振直接测定。F-19核是一种很有前途的标记，可以克服H-2、C-13或N-15的低灵敏度，并作为生物化合物的无背景报告基团。为了使固态F-19核磁共振的优势充分用于多肽的结构研究，我们系统地测量了最相关的芳香族和脂肪族F-19标记氨基酸的化学位移各向异性和弛豫性质。在这连续两篇文章的第一部分中，通过静态和MAS实验表征了6个不同的f -19取代基在代表性芳香侧链上的多晶粉末。这些数据还与合成肽中含有的相同氨基酸的结果进行了比较。光谱显示出各种各样的线形，从中提取了CSA张量的主值。此外，通过F-19核磁共振测定了固态中温度相关的T-1和T-2弛豫时间，并在溶液中获得了各向同性化学位移和标量耦合。(C) 2007爱思唯尔公司版权所有。
Structural parameters of peptides and proteins in biomembranes can be directly measured by solid state NMR of selectively labeled amino acids. The F-19 nucleus is a promising label to overcome the low sensitivity of H-2, C-13 or N-15, and to serve as a background-free reporter group in biological compounds. To make the advantages of solid state F-19 NMR fully available for structural studies of polypeptides, we have systematically measured the chemical shift anisotropies and relaxation properties of the most relevant aromatic and aliphatic F-19-labeled amino acids. In this first part of two consecutive contributions, six different F-19-substituents on representative aromatic side chains were characterized as polycrystalline powders by static and MAS experiments. The data are also compared with results on the same amino acids incorporated in synthetic peptides. The spectra show a wide variety of lineshapes, from which the principal values of the CSA tensors were extracted. In addition, temperature-dependent T-1 and T-2 relaxation times were determined by F-19 NMR in the solid state, and isotropic chemical shifts and scalar couplings were obtained in solution. (C) 2007 Elsevier Inc. All rights reserved.