Application of iterative soft thresholding for fast reconstruction of NMR data non-uniformly sampled with multidimensional Poisson Gap scheduling [0.03%]
迭代软阈值法在多维泊松间隙调度非均匀采样核磁共振数据快速重建中的应用
Sven G Hyberts,Alexander G Milbradt,Andreas B Wagner et al.
Sven G Hyberts et al.
The fast Fourier transformation has been the gold standard for transforming data from time to frequency domain in many spectroscopic methods, including NMR. While reliable, it has as a drawback that it requires a grid of uniformly sampled d...
Mads Kristian Erlin Nygaard,Anders Schou Andersen,Hans-Henrik Kristensen et al.
Mads Kristian Erlin Nygaard et al.
Redox-dependent conformational changes in eukaryotic cytochromes revealed by paramagnetic NMR spectroscopy [0.03%]
顺磁NMR光谱揭示出氧化还原依赖的真核细胞细胞色素构象变化
Alexander N Volkov,Sophie Vanwetswinkel,Karen Van de Water et al.
Alexander N Volkov et al.
Cytochrome c (Cc) is a soluble electron carrier protein, transferring reducing equivalents between Cc reductase and Cc oxidase in eukaryotes. In this work, we assessed the structural differences between reduced and oxidized Cc in solution b...
Combining NMR ensembles and molecular dynamics simulations provides more realistic models of protein structures in solution and leads to better chemical shift prediction [0.03%]
结合NMR集合和分子动力学模拟可提供更真实的溶液中蛋白质结构模型并可更好地预测化学位移值
Juuso Lehtivarjo,Kari Tuppurainen,Tommi Hassinen et al.
Juuso Lehtivarjo et al.
While chemical shifts are invaluable for obtaining structural information from proteins, they also offer one of the rare ways to obtain information about protein dynamics. A necessary tool in transforming chemical shifts into structural and...
Vitaliy Y Gorbatyuk,Martin R Schiller,Oksana I Gorbatyuk et al.
Vitaliy Y Gorbatyuk et al.
Estimating side-chain order in methyl-protonated, perdeuterated proteins via multiple-quantum relaxation violated coherence transfer NMR spectroscopy [0.03%]
利用违反相干转移NMR光谱法估算甲基质子化、全氘代蛋白质侧链的有序性
Hechao Sun,Raquel Godoy-Ruiz,Vitali Tugarinov
Hechao Sun
Relaxation violated coherence transfer NMR spectroscopy (Tugarinov et al. in J Am Chem Soc 129:1743-1750, 2007) is an established experimental tool for quantitative estimation of the amplitudes of side-chain motions in methyl-protonated, hi...
Identification of helix capping and b-turn motifs from NMR chemical shifts [0.03%]
基于核磁共振化学位移的螺旋帽和β-发夹识别
Yang Shen,Ad Bax
Yang Shen
We present an empirical method for identification of distinct structural motifs in proteins on the basis of experimentally determined backbone and (13)C(β) chemical shifts. Elements identified include the N-terminal and C-terminal helix ca...
Combinatorial triple-selective labeling as a tool to assist membrane protein backbone resonance assignment [0.03%]
组合三重选择性标记在协助膜蛋白主链共振指认方面的工具
Frank Löhr,Sina Reckel,Mikhail Karbyshev et al.
Frank Löhr et al.
Obtaining NMR assignments for slowly tumbling molecules such as detergent-solubilized membrane proteins is often compromised by low sensitivity as well as spectral overlap. Both problems can be addressed by amino-acid specific isotope label...
A procedure to validate and correct the 13C chemical shift calibration of RNA datasets [0.03%]
一种验证和校正RNA数据集的碳-13化学位移标度的方法
Thomas Aeschbacher,Mario Schubert,Frédéric H-T Allain
Thomas Aeschbacher
Chemical shifts reflect the structural environment of a certain nucleus and can be used to extract structural and dynamic information. Proper calibration is indispensable to extract such information from chemical shifts. Whereas a variety o...
Efficient sequential assignments in proteins with reduced dimensionality 3D HN(CA)NH [0.03%]
三维HN(CA)NH高效顺序分配简化蛋白质维度
Kousik Chandra,Garima Jaipuria,Divya Shet et al.
Kousik Chandra et al.
We present reduced dimensionality (RD) 3D HN(CA)NH for efficient sequential assignment in proteins. The experiment correlates the (15)N and (1)H chemical shift of a residue ('i') with those of its immediate N-terminal (i - 1) and C-terminal...