The Impact of Hydrogen Bonding on Amide H-1 Chemical Shift Anisotropy Studied by Cross-Correlated Relaxation and Liquid Crystal NMR Spectroscopy

doi:10.1021/ja103629e

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	The Impact of Hydrogen Bonding on Amide H-1 Chemical Shift Anisotropy Studied by Cross-Correlated Relaxation and Liquid Crystal NMR Spectroscopy
	Yao, Lishan1,2 ; Grishaev, Alexander 1; Cornilescu, Gabriel 3; Bax, Ad 1
	2010-08-11
发表期刊	JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷号	132 期号:31 页码:10866-10875
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.
文章类型	Article
WOS标题词	Science & Technology ; Physical Sciences
DOI	10.1021/ja103629e
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研究方向	Chemistry
WOS类目	Chemistry, Multidisciplinary
WOS记录号	WOS:000280692200047
引用统计
文献类型	期刊论文
条目标识符	http://ir.qibebt.ac.cn/handle/337004/6538
专题	蛋白质设计研究组
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.