Multiplet-filtered and gradient-selected zero-quantum TROSY experiments for 13C1H3 methyl groups in proteins [0.03%]
用于蛋白质中13C1H3甲基的多组分裂和梯度选择零量子TROSY实验
Michelle L Gill,Arthur G Palmer rd
Michelle L Gill
Multiplet-filtered and gradient-selected heteronuclear zero-quantum coherence (gsHZQC) TROSY experiments are described for measuring (1)H-(13)C correlations for (13)CH(3) methyl groups in proteins. These experiments provide improved suppres...
Rapid measurement of residual dipolar couplings for fast fold elucidation of proteins [0.03%]
快速测定残留偶极耦合以快捷阐明蛋白质折叠状态
Rodolfo M Rasia,Ewen Lescop,Javier F Palatnik et al.
Rodolfo M Rasia et al.
It has been demonstrated that protein folds can be determined using appropriate computational protocols with NMR chemical shifts as the sole source of experimental restraints. While such approaches are very promising they still suffer from ...
Structure, dynamics, and ionization equilibria of the tyrosine residues in Bacillus circulans xylanase [0.03%]
芽孢杆菌木聚糖酶酪氨酸残基的结构、动力学及离子化平衡研究
Simon J Baturin,Mark Okon,Lawrence P McIntosh
Simon J Baturin
We have developed NMR spectroscopic methods to investigate the tyrosines within Bacillus circulans xylanase (BcX). Four slowly exchanging buried tyrosine hydroxyl protons with chemical shifts between 7.5 and 12.5 ppm were found using a long...
Cys-Ph-TAHA: a lanthanide binding tag for RDC and PCS enhanced protein NMR [0.03%]
一种新的半胱氨酸标签 Ph-Cys-TAHA 用于增强蛋白质的残基距离变化和各向异性变化测量
Fabian Peters,Mitcheell Maestre-Martinez,Andrei Leonov et al.
Fabian Peters et al.
Here we present Cys-Ph-TAHA, a new nonadentate lanthanide tag for the paramagnetic labelling of proteins. The tag can be easily synthesized and is stereochemically homogenous over a wide range of temperatures, yielding NMR spectra with a si...
Sishi Tang,David A Case
Sishi Tang
Individual peptide groups in proteins must exhibit some variation in the chemical shift anisotropy (CSA) of their constituent atoms, but not much is known about the extent or origins of this dispersion. Direct spectroscopic measurement of C...
Biomolecular structure refinement using the GROMOS simulation software [0.03%]
基于GROMOS模拟软件的生物大分子结构优化-refinement of biomolecular structures using gromos simulation package
Nathan Schmid,Jane R Allison,Jožica Dolenc et al.
Nathan Schmid et al.
For the understanding of cellular processes the molecular structure of biomolecules has to be accurately determined. Initial models can be significantly improved by structure refinement techniques. Here, we present the refinement methods an...
G Marius Clore
G Marius Clore
While an extensive body of knowledge has accumulated on the structures of transcription factors, DNA and their complexes from both NMR and crystallography, much less is known at a molecular level regarding the mechanisms whereby transcripti...
Narrowing the conformational space sampled by two-domain proteins with paramagnetic probes in both domains [0.03%]
利用两个结构域内的顺磁探针缩小两个结构域蛋白质采样的构象空间
Soumyasri Dasgupta,Xiaoyu Hu,Peter H J Keizers et al.
Soumyasri Dasgupta et al.
Calmodulin is a two-domain protein which in solution can adopt a variety of conformations upon reorientation of its domains. The maximum occurrence (MO) of a set of calmodulin conformations that are representative of the overall conformatio...
Cryogenic temperature effects and resolution upon slow cooling of protein preparations in solid state NMR [0.03%]
固体状态下蛋白质试样缓慢冷却对核磁共振谱的影响及分辨率效应
Arne H Linden,W Trent Franks,Ümit Akbey et al.
Arne H Linden et al.
X-ray crystallography using synchrotron radiation and the technique of dynamic nuclear polarization (DNP) in nuclear magnetic resonance (NMR) require samples to be kept at temperatures below 100 K. Protein dynamics are poorly understood bel...
Evaluation of the influence of intermolecular electron-nucleus couplings and intrinsic metal binding sites on the measurement of 15N longitudinal paramagnetic relaxation enhancements in proteins by solid-state NMR [0.03%]
评估分子间电子-核耦合及固有金属结合位点对蛋白质中固体状态NMR测量纵向顺磁弛豫增强的影响
Philippe S Nadaud,Ishita Sengupta,Jonathan J Helmus et al.
Philippe S Nadaud et al.
Magic-angle spinning solid-state NMR measurements of (15)N longitudinal paramagnetic relaxation enhancements (PREs) in (13)C,(15)N-labeled proteins modified with Cu(2+)-chelating tags can yield multiple long-range electron-nucleus distance ...