On the use of 3J-coupling NMR data to derive structural information on proteins [0.03%]
关于利用三重J耦合核磁共振数据推导蛋白质结构信息的使用
Lorna J Smith,Wilfred F van Gunsteren,Bartosz Stankiewicz et al.
Lorna J Smith et al.
Values of 3J-couplings as obtained from NMR experiments on proteins cannot easily be used to determine protein structure due to the difficulty of accounting for the high sensitivity of intermediate 3J-coupling values (4-8 Hz) to the averagi...
Detecting aspartate isomerization and backbone cleavage after aspartate in intact proteins by NMR spectroscopy [0.03%]
利用核磁共振光谱法检测蛋白质完整蛋白天冬氨酸异构化和主链断裂现象
Arthur Hinterholzer,Vesna Stanojlovic,Christof Regl et al.
Arthur Hinterholzer et al.
The monitoring of non-enzymatic post-translational modifications (PTMs) in therapeutic proteins is important to ensure drug safety and efficacy. Together with methionine and asparagine, aspartic acid (Asp) is very sensitive to spontaneous a...
Correction to: A suite of 19F based relaxation dispersion experiments to assess biomolecular motions [0.03%]
Correction to: 一组基于 19F 的弛豫分散实验以评估生物分子运动
Jan H Overbeck,Werner Kremer,Remco Sprangers
Jan H Overbeck
In the original publication, Figures 3 and 6 were displayed incorrectly due to a mistake made by the publisher. The correct version of Figs. 3 and 6 are given below.
Published Erratum
Journal of biomolecular NMR. 2020 Dec;74(12):767-768. DOI:10.1007/s10858-020-00352-8 2020
Raymond S Norton,Wolfgang Jahnke
Raymond S Norton
The article "Boeszoermenyi A, Ogórek B, Jain A, Arthanari H, Wagner G (2020) The precious fluorine on the ring: fluorine NMR for biological systems. J Biomol NMR. https ://doi.org/10.1007/s10858-020-00331-z" was written for the "Special Is...
Published Erratum
Journal of biomolecular NMR. 2020 Nov;74(10-11):477. DOI:10.1007/s10858-020-00351-9 2020
Sebastian Hiller
Sebastian Hiller
Advanced NMR methods combined with biophysical techniques have recently provided unprecedented insight into structure and dynamics of molecular chaperones and their interaction with client proteins. These studies showed that several molecul...
HACANCOi: a new Hα-detected experiment for backbone resonance assignment of intrinsically disordered proteins [0.03%]
HACANCOi：一种新的Hα检测实验，用于固有无序蛋白质主链共振分配
Mikael Karjalainen,Helena Tossavainen,Maarit Hellman et al.
Mikael Karjalainen et al.
Unidirectional coherence transfer is highly efficient in intrinsically disordered proteins (IDPs). Their elevated ps-ns timescale dynamics ensures long transverse (T2) relaxation times allowing sophisticated coherence transfer pathway selec...
RING NMR dynamics: software for analysis of multiple NMR relaxation experiments [0.03%]
环NMR动力学：用于多NMR弛豫实验分析的软件
Martha A Beckwith,Teddy Erazo-Colon,Bruce A Johnson
Martha A Beckwith
Molecular motions are fundamental to the existence of life, and NMR spectroscopy remains one of the most useful and powerful methods to measure their rates and molecular characteristics. Multiple experimental methods are available for measu...
Optimized selection of slow-relaxing 13C transitions in methyl groups of proteins: application to relaxation dispersion [0.03%]
蛋白质甲基团中缓慢弛豫的13C跃迁的优化选择：在弛豫色散中的应用
Vitali Tugarinov,Theodoros K Karamanos,G Marius Clore
Vitali Tugarinov
Optimized selection of the slow-relaxing components of single-quantum 13C magnetization in 13CH3 methyl groups of proteins using acute (< 90°) angle 1H radio-frequency pulses, is described. The optimal selection scheme is more relaxation-t...
A suite of 19F based relaxation dispersion experiments to assess biomolecular motions [0.03%]
一套基于19F的松弛色散实验来评估生物大分子运动
Jan H Overbeck,Werner Kremer,Remco Sprangers
Jan H Overbeck
Proteins and nucleic acids are highly dynamic bio-molecules that can populate a variety of conformational states. NMR relaxation dispersion (RD) methods are uniquely suited to quantify the associated kinetic and thermodynamic parameters. He...
The methyl 13C-edited/13C-filtered transferred NOE for studying protein interactions with short linear motifs [0.03%]
用于研究蛋白质与短线性基序相互作用的甲基13C编辑/13C过滤转移NOE
Suresh Kumar,Sabine R Akabayov,Naama Kessler et al.
Suresh Kumar et al.
Many proteins interact with their ligand proteins by recognition of short linear motifs that are often intrinsically disordered. These interactions are usually weak and are characterized by fast exchange. NMR spectroscopy is a powerful tool...