Correction: Measuring long-range contacts in a fully protonated protein at 105 kHz magic angle spinning [0.03%]
订正：在105kHz全质子魔角旋转条件下测定蛋白质长程接触
Zainab O Mustapha,Eren H Ozturk,Benjamin E Lefkin et al.
Zainab O Mustapha et al.
Published Erratum
Journal of biomolecular NMR. 2025 Nov 21. DOI:10.1007/s10858-025-00478-7 2025
Side-chain-selective deuterium labeling by a simple bio-expression method enhances resolution and simplifies spectra in 1H-detected protein solid-state NMR [0.03%]
利用简单的生物表达方法对蛋白质进行侧链选择性氘标记可提高固态NMR谱分辨率并简化谱图
Yoshiki Shigemitsu,Yuki Miyazaki,Hibiki Terami et al.
Yoshiki Shigemitsu et al.
We present a novel approach for side-chain-selective deuteration of proteins to improve 1Hα spectral resolution and to simplify side-chain signals in 1H-detected protein solid-state NMR (SSNMR) with a simple bio-expression method using E. ...
Correction: Quantifying protein-drug lifetimes in human cells by 19F NMR spectroscopy [0.03%]
关于校正：通过19F NMR光谱量化人体细胞中的蛋白质-药物寿命
Wenkai Zhu,Fatema Bhinderwala,Sarah Rambo et al.
Wenkai Zhu et al.
Published Erratum
Journal of biomolecular NMR. 2025 Oct 8. DOI:10.1007/s10858-025-00473-y 2025
Measuring long-range contacts in a fully protonated protein at 105 kHz magic angle spinning [0.03%]
在105kHz高倾角旋转条件下测量完全质子化的蛋白质中的长程相互作用
Zainab O Mustapha,Eren H Ozturk,Benjamin E Lefkin et al.
Zainab O Mustapha et al.
The use of 1H detection, made possible by very fast magic-angle spinning (MAS), has revolutionized the field of biomolecular solid-state NMR. In the past, 1H detection was often paired with deuteration schemes to achieve the highest possibl...
Analyzing sub-millisecond timescale protein dynamics using eCPMG experiments [0.03%]
利用eCPMG实验分析亚毫秒时间尺度的蛋白质动力学
Apurva Phale,Aishani Tewari,Gayatri Tendulkar et al.
Apurva Phale et al.
Cellular functions require biomolecules to transition among various conformational sub-states in the energy landscape. A mechanistic understanding of cellular functions requires quantitative knowledge of the kinetics, thermodynamics, and st...
An optimized 13C single-quantum CPMG relaxation dispersion experiment for investigating microsecond-to-millisecond timescale dynamics in large proteins [0.03%]
一种优化的单量子CPMG弛豫离散实验用于研究大蛋白质中的微秒到毫秒尺度的动力学现象
Tairan Yuwen,Jiangshu Liu,Zhilian Xia et al.
Tairan Yuwen et al.
Biomolecular dynamics in the microsecond-to-millisecond (µs-ms) timescale are linked to various biological functions, such as enzyme catalysis, allosteric regulation, and ligand recognition. In solution state NMR, Carr-Purcell-Meiboom-Gill...
Divide-and-conquer strategy for NMR studies of the E. coli γ-clamp loader complex [0.03%]
分而治之策略在大肠杆菌γ-钳夹加载复合物的核磁共振研究中的应用
Sam Mahdi,Irina V Semenova,Irina Bezsonova et al.
Sam Mahdi et al.
The E. coli γ-clamp loader is a 200 kDa pentameric AAA + ATPase comprised of γ, δ and δ' subunits in a 3:1:1 ratio, which opens the ring shaped β-clamp homodimer and loads it onto DNA in a process essential for DNA replication. The cla...
Investigating structural and dynamic changes in cellulose due to nanocrystallization [0.03%]
纳米结晶化对纤维素结构和动力学影响的研究
Bijay Laxmi Pradhan,Prince Sen,Krishna Kishor Dey et al.
Bijay Laxmi Pradhan et al.
Cellulose nanocrystals (CNCs) is synthesized from alpha-cellulose by acid hydrolysis method, and formation of nanocrystallization is comprised by using various microscopic and spectroscopic techniques like PXRD, XPS, Raman, FTIR, PL, UV-Vis...
Extending the detectable time window of fast protein dynamics using 1HN E-CPMG [0.03%]
利用1HN E-CPMG延长快速蛋白质动态的检测时间窗口
Dwaipayan Mukhopadhyay,Supriya Pratihar,Stefan Becker et al.
Dwaipayan Mukhopadhyay et al.
Recent advances in high power NMR relaxation dispersion experiments have significantly enhanced our ability to study fast µs timescale motions in proteins, which are crucial for understanding their biological functions. Here, we have exten...
Estimating cross-relaxation rates between methyl and neighboring labile proton spins in high molecular weight proteins [0.03%]
高分子量蛋白质中甲基和邻近亚胺质子自旋之间交叉弛豫率的估计
Vitali Tugarinov,G Marius Clore
Vitali Tugarinov
We show that water saturation leads to deleterious losses in sensitivity of methyl signals in selectively methyl-[13CH3]-labeled protein samples of high molecular weight proteins dissolved in H2O. These losses arise from efficient cross-rel...