Evaluation of TOCSY mixing for sensitivity-enhancement in solid-state NMR and application of 4D experiments for side-chain assignments of the full-length 30 kDa membrane protein GlpG [0.03%]
TOCSY混合用于固态NMR灵敏度增强的评价及4D实验在全长30kDa膜蛋白GlpG侧链指认中的应用
Carl Öster,Veniamin Chevelkov,Adam Lange
Carl Öster
Chemical shift assignments of large membrane proteins by solid-state NMR experiments are challenging. Recent advancements in sensitivity-enhanced pulse sequences, have made it feasible to acquire 1H-detected 4D spectra of these challenging ...
15N-detected TROSY for 1H-15N heteronuclear correlation to study intrinsically disordered proteins: strategies to increase spectral quality [0.03%]
利用15N直接检测的TROSY进行研究固有无序蛋白的1H-15N异核相关光谱：提高谱图质量的方法
Maria Anna Rodella,Robert Schneider,Rainer Kümmerle et al.
Maria Anna Rodella et al.
Intrinsically disordered proteins and protein regions are central to many biological processes but difficult to characterize at atomic resolution. Nuclear magnetic resonance is particularly well-suited for providing structural and dynamical...
Alpha-helices as alignment reporters in residual dipolar coupling analysis of proteins [0.03%]
残余偶极耦合分析蛋白质中的α-螺旋构象报告单元
Yang Shen,Marshall J Smith,John M Louis et al.
Yang Shen et al.
Inclusion of residual dipolar couplings (RDCs) during the early rounds of protein structure determination requires use of a floating alignment tensor or knowledge of the alignment tensor strength and rhombicity. For proteins with interdomai...
Using temperature coefficients to support resonance assignment of intrinsically disordered proteins [0.03%]
利用温度系数支持固有无序蛋白的共振 assignments
Paulina Putko,Javier Agustin Romero,Christian F Pantoja et al.
Paulina Putko et al.
The resonance assignment of large intrinsically disordered proteins (IDPs) is difficult due to the low dispersion of chemical shifts (CSs). Luckily, CSs are often specific for certain residue types, which makes the task easier. Our recent w...
Perspective: on the importance of extensive, high-quality and reliable deposition of biomolecular NMR data in the age of artificial intelligence [0.03%]
观点：在人工智能时代广泛、高质量和可靠地沉积生物分子NMR数据的重要性
Victoria A Higman,Eliza Płoskoń,Gary S Thompson et al.
Victoria A Higman et al.
Artificial intelligence (AI) models are revolutionising scientific data analysis but are reliant on large training data sets. While artificial training data can be used in the context of NMR processing and data analysis methods, relating NM...
19F NMR relaxation of buried tryptophan side chains suggest anisotropic rotational diffusion of the protein RfaH [0.03%]
埋藏的色氨酸侧链的NMR弛豫表明蛋白质RfaH各向异性的旋转扩散
Md Khushnood Alam,R Aishwarya Bhuvaneshwari,Ishita Sengupta
Md Khushnood Alam
The recent application of 19F NMR in the study of biomolecular structure and dynamics has made it a potentially attractive probe to complement traditional 15N/13C labelled probes for backbone and sidechain dynamics, albeit with some complic...
Pitfalls in measurements of R1 relaxation rates of protein backbone 15N nuclei [0.03%]
关于蛋白质主链$^{15}$N核R1弛豫率测量的陷阱
Vladlena Kharchenko,Samah Al-Harthi,Andrzej Ejchart et al.
Vladlena Kharchenko et al.
The dynamics of the backbone and side-chains of protein are routinely studied by interpreting experimentally determined 15N spin relaxation rates. R1(15N), the longitudinal relaxation rate, reports on fast motions and encodes, together with...
Towards cost-effective side-chain isotope labelling of proteins expressed in human cells [0.03%]
利用人体细胞表达蛋白质实现成本效益的侧链同位素标记方法
Martina Rosati,Letizia Barbieri,Matus Hlavac et al.
Martina Rosati et al.
Side chain isotope labelling is a powerful tool to study protein structure and interactions by NMR spectroscopy. 1H,13C labelling of side-chain methyl groups in a deuterated background allows studying large molecules, while side-chain aroma...
Henry T P Annecke,Reiner Eidelpes,Hannes Feyrer et al.
Henry T P Annecke et al.
Understanding the structure and function of nucleic acids in their native environment is crucial to structural biology and one focus of in-cell NMR spectroscopy. Many challenges hamper in-cell NMR in human cell lines, e.g. sample decay thro...
Transverse relaxation optimized spectroscopy of NH2 groups in glutamine and asparagine side chains of proteins [0.03%]
蛋白质中谷氨酰胺和天冬酰胺侧链NH2基团的横向弛豫优化谱学研究
Vitali Tugarinov,Francesco Torricella,Jinfa Ying et al.
Vitali Tugarinov et al.
A transverse relaxation optimized spectroscopy (TROSY) approach is described for the optimal detection of NH2 groups in asparagine and glutamine side chains of proteins. Specifically, we have developed NMR experiments for isolating the slow...