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期刊名:Journal of biomolecular nmr

缩写:J BIOMOL NMR

ISSN:0925-2738

e-ISSN:1573-5001

IF/分区:2.1/Q2

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共收录本刊相关文章索引1194条
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Talia Fargason,Ting Wang,Naiduwadura Ivon Upekala De Silva et al. Talia Fargason et al.
Residual dipolar couplings (RDCs) provide valuable NMR parameters that can be used for structural calculation and verification. Measuring RDCs requires aligning macromolecules using one of various types of alignment media. Of different alig...
Gregory L Olsen,Or Szekely,Borja Mateos et al. Gregory L Olsen et al.
Signal enhancements of up to two orders of magnitude in protein NMR can be achieved by employing HDO as a vector to introduce hyperpolarization into folded or intrinsically disordered proteins. In this approach, hyperpolarized HDO produced ...
Matthias Dreydoppel,Heiner N Raum,Ulrich Weininger Matthias Dreydoppel
Ring flips of phenylalanine and tyrosine are a hallmark of protein dynamics. They report on transient breathing motions of proteins. In addition, flip rates also depend on stabilizing interactions in the ground state, like aromatic stacking...
Jingjing Lu,Fengmei Zhou,Wanhui Liu et al. Jingjing Lu et al.
Arginine side chains play critical roles in many protein-ligand interactions and enzyme catalysis. Unambiguous resonance assignment is a prerequisite for the nuclear magnetic resonance (NMR) spectroscopy studies of arginine side chains dyna...
Takuma Kasai,Shunsuke Ono,Seizo Koshiba et al. Takuma Kasai et al.
Signal overlapping is a major bottleneck for protein NMR analysis. We propose a new method, stable-isotope-assisted parameter extraction (SiPex), to resolve overlapping signals by a combination of amino-acid selective isotope labeling (AASI...
Zuzana Jaseňáková,Vojtěch Zapletal,Petr Padrta et al. Zuzana Jaseňáková et al.
Improving our understanding of nanosecond motions in disordered proteins requires the enhanced sampling of the spectral density function obtained from relaxation at low magnetic fields. High-resolution relaxometry and two-field NMR measurem...
Theodoros K Karamanos,Vitali Tugarinov,G Marius Clore Theodoros K Karamanos
Modelling of protein structures based on backbone chemical shifts, using programs such as CS-ROSETTA, is becoming increasingly popular, especially for systems where few restraints are available or where homologous structures are already kno...
Helena Tossavainen,Santeri Salovaara,Maarit Hellman et al. Helena Tossavainen et al.
Resonance assignment of intrinsically disordered proteins is remarkably challenging due to scant chemical shift dispersion arising from conformational heterogeneity. The challenge is even greater if repeating segments are present in the ami...
Christopher A Waudby,Margaux Ouvry,Ben Davis et al. Christopher A Waudby et al.
NMR spectroscopy provides a powerful approach for the characterisation of chemical exchange and molecular interactions by analysis of series of experiments acquired over the course of a titration measurement. The appearance of NMR resonance...
Ian M Robertson,Brittney A Klein,Brian D Sykes Ian M Robertson
When planning a fluorine labeling strategy for 19F solid state NMR (ssNMR) studies of the structure and/or mobility of fluorine labeled compounds in situ in an oriented biological system, it is important to characterize the NMR properties o...