Paweł Kasprzak,Mateusz Urbańczyk,Krzysztof Kazimierczuk
Paweł Kasprzak
Non-uniform sampling (NUS) is a popular way of reducing the amount of time taken by multidimensional NMR experiments. Among the various non-uniform sampling schemes that exist, the Poisson-gap (PG) schedules are particularly popular, especi...
Efficient solvent suppression with adiabatic inversion for 1H-detected solid-state NMR [0.03%]
用于固态氢核检测核磁共振的溶剂高效抑制的绝热反转方法
Tatsuya Matsunaga,Ryotaro Okabe,Yoshitaka Ishii
Tatsuya Matsunaga
This study introduces a conceptually new solvent suppression scheme with adiabatic inversion pulses for 1H-detected multidimensional solid-state NMR (SSNMR) of biomolecules and other systems, which is termed "Solvent suppression of Liquid s...
Correction to: An automated iterative approach for protein structure refinement using pseudocontact shifts [0.03%]
校正：使用伪接触移来精炼蛋白质结构的自动化迭代方法
Stefano Cucuzza,Peter Güntert,Andreas Plückthun et al.
Stefano Cucuzza et al.
Published Erratum
Journal of biomolecular NMR. 2021 Dec;75(10-12):429-430. DOI:10.1007/s10858-021-00378-6 2021
A simple and sensitive detection of the binding ligands by using the receptor aggregation and NMR spectroscopy: a test case of the maltose binding protein [0.03%]
通过受体聚集和核磁共振光谱法简单灵敏地检测配体结合：麦芽糖结合蛋白的测试案例
Young Kee Chae,Yoonjin Um,Hakbeom Kim
Young Kee Chae
Protein-ligand interaction is one of the highlights of molecular recognition. The most popular application of this type of interaction is drug development which requires a high throughput screening of a ligand that binds to the target prote...
Matthias Dreydoppel,Roman J Lichtenecker,Mikael Akke et al.
Matthias Dreydoppel et al.
Aromatic side chains are attractive probes of protein dynamic, since they are often key residues in enzyme active sites and protein binding sites. Dynamic processes on microsecond to millisecond timescales can be studied by relaxation dispe...
CSI-LSTM: a web server to predict protein secondary structure using bidirectional long short term memory and NMR chemical shifts [0.03%]
基于双向长短时记忆和NMR化学位移的蛋白质二级结构预测服务器(CSI-LSTM)
Zhiwei Miao,Qianqian Wang,Xiongjie Xiao et al.
Zhiwei Miao et al.
Protein secondary structure provides rich structural information, hence the description and understanding of protein structure relies heavily on it. Identification or prediction of secondary structures therefore plays an important role in p...
Evaluation of the tert-butyl group as a probe for NMR studies of macromolecular complexes [0.03%]
叔丁基作为研究大分子复合物的NMR探针的评价研究
Rashmi Voleti,Sofia Bali,Jaime Guerrero et al.
Rashmi Voleti et al.
The development of methyl transverse relaxation optimized spectroscopy has greatly facilitated the study of macromolecular assemblies by solution NMR spectroscopy. However, limited sample solubility and stability has hindered application of...
TRACT revisited: an algebraic solution for determining overall rotational correlation times from cross-correlated relaxation rates [0.03%]
重温TRACT法：通过交叉相关弛豫率确定整体旋转关联时间的代数解法
Scott A Robson,Çağdaş Dağ,Hongwei Wu et al.
Scott A Robson et al.
Accurate rotational correlation times ([Formula: see text]) are critical for quantitative analysis of fast timescale NMR dynamics. As molecular weights increase, the classic derivation of [Formula: see text] using transverse and longitudina...
Off-resonance 13C-2H REDOR NMR for site-resolved studies of molecular motion [0.03%]
离共振13C-2H REDOR核磁共振用于分子运动的位点分辨研究
Martin D Gelenter,Kelly J Chen,Mei Hong
Martin D Gelenter
We introduce a 13C-2H Rotational Echo DOuble Resonance (REDOR) technique that uses the difference between on-resonance and off-resonance 2H irradiation to detect dynamic segments in deuterated molecules. By selectively inverting specific re...
An automated iterative approach for protein structure refinement using pseudocontact shifts [0.03%]
一种基于伪接触位移的蛋白质结构优化的自动迭代方法
Stefano Cucuzza,Peter Güntert,Andreas Plückthun et al.
Stefano Cucuzza et al.
NMR structure calculation using NOE-derived distance restraints requires a considerable number of assignments of both backbone and sidechains resonances, often difficult or impossible to get for large or complex proteins. Pseudocontact shif...