The Impact of Hydrogen Bonding on Amide H-1 Chemical Shift Anisotropy Studied by Cross-Correlated Relaxation and Liquid Crystal NMR Spectroscopy
文献类型：期刊论文
| 作者 | Yao, Lishan1,2 ; Grishaev, Alexander1; Cornilescu, Gabriel3; Bax, Ad1
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| 刊名 | JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
 |
| 出版日期 | 2010-08-11 |
| 卷号 | 132期号:31页码:10866-10875 |
| 英文摘要 | Site-specific H-1 chemical shift anisotropy (CSA) tensors have been derived for the well-ordered backbone amide moieties in the B3 domain of protein G (GB3). Experimental input data include residual chemical shift anisotropy (RCSA), measured in six mutants that align differently relative to the static magnetic field when dissolved in a liquid crystalline Pf1 suspension, and cross-correlated relaxation rates between the H-1(N) CSA tensor and either the H-1-N-15, the H-1-C-13', or the H-1-C-13(alpha) dipolar interactions. Analyses with the assumption that the H-1(N) CSA tensor is symmetric with respect to the peptide plane (three-parameter fit) or without this premise (five-parameter fit) yield very similar results, confirming the robustness of the experimental input data, and that, to a good approximation, one of the principal components orients orthogonal to the peptide plane. H-1(N) CSA tensors are found to deviate strongly from axial symmetry, with the most shielded tensor component roughly parallel to the N-H vector, and the least shielded component orthogonal to the peptide plane. DFT calculations on pairs of N-methyl acetamide and acetamide in H-bonded geometries taken from the GB3 X-ray structure correlate with experimental data and indicate that H-bonding effects dominate variations in the H-1(N) CSA. Using experimentally derived H-1(N) CSA tensors, the optimal relaxation interference effect needed for narrowest H-1(N) TROSY line widths is found at similar to 1200 MHz. |
| WOS标题词 | Science & Technology ; Physical Sciences |
| 类目[WOS] | Chemistry, Multidisciplinary |
| 研究领域[WOS] | Chemistry |
| 关键词[WOS] | NUCLEAR-MAGNETIC-RESONANCE ; DENSITY-FUNCTIONAL CALCULATIONS ; PROTEIN-STRUCTURE VALIDATION ; STATE C-13 NMR ; SOLID-STATE ; MICROCRYSTALLINE PROTEIN ; CONSERVATIVE MUTAGENESIS ; DIPOLAR COUPLINGS ; BINDING DOMAIN ; L-ALANINE |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000280692200047 |
| 公开日期 | 2015-12-24 |
| 源URL | [http://ir.qibebt.ac.cn/handle/337004/6538]  |
| 专题 | 青岛生物能源与过程研究所_仿真模拟团队 |
| 作者单位 | 1.NIDDK, Chem Phys Lab, NIH, Bethesda, MD 20892 USA 2.Chinese Acad Sci, Qingdao Inst Bioenergy & Bioproc Technol, Qingdao 266061, Peoples R China 3.Natl Magnet Resonance Facil, Madison, WI 53706 USA |
| 推荐引用方式 GB/T 7714 | Yao, Lishan,Grishaev, Alexander,Cornilescu, Gabriel,et al. The Impact of Hydrogen Bonding on Amide H-1 Chemical Shift Anisotropy Studied by Cross-Correlated Relaxation and Liquid Crystal NMR Spectroscopy[J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY,2010,132(31):10866-10875. |
| APA | Yao, Lishan,Grishaev, Alexander,Cornilescu, Gabriel,&Bax, Ad.(2010).The Impact of Hydrogen Bonding on Amide H-1 Chemical Shift Anisotropy Studied by Cross-Correlated Relaxation and Liquid Crystal NMR Spectroscopy.JOURNAL OF THE AMERICAN CHEMICAL SOCIETY,132(31),10866-10875. |
| MLA | Yao, Lishan,et al."The Impact of Hydrogen Bonding on Amide H-1 Chemical Shift Anisotropy Studied by Cross-Correlated Relaxation and Liquid Crystal NMR Spectroscopy".JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 132.31(2010):10866-10875. |
入库方式： OAI收割
来源：青岛生物能源与过程研究所
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