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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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Rasmus Linser Rasmus Linser
Proteins with excessive deuteration give access to proton detected solid-state NMR spectra of extraordinary resolution and sensitivity. The high spectral quality achieved after partial proton back-exchange has been shown to start a new era ...
Carolyn B Lauzon,Peter van Zijl,James T Stivers Carolyn B Lauzon
Chemical Exchange Saturation Transfer (CEST) is an MRI approach that can indirectly detect exchange broadened protons that are invisible in traditional NMR spectra. We modified the CEST pulse sequence for use on high-resolution spectrometer...
Birgit Habenstein,Christian Wasmer,Luc Bousset et al. Birgit Habenstein et al.
We present the de novo resonance assignments for the crystalline 33 kDa C-terminal domain of the Ure2 prion using an optimized set of five 3D solid-state NMR spectra. We obtained, using a single uniformly (13)C, (15)N labeled protein sample...
Xinying Jia,Hiromasa Yagi,Xun-Cheng Su et al. Xinying Jia et al.
Paramagnetic relaxation enhancements from unpaired electrons observed in nuclear magnetic resonance (NMR) spectra present powerful long-range distance restraints. The most frequently used paramagnetic tags, however, are tethered to the prot...
Aleksandr B Sahakyan,Wim F Vranken,Andrea Cavalli et al. Aleksandr B Sahakyan et al.
Protein methyl groups have recently been the subject of much attention in NMR spectroscopy because of the opportunities that they provide to obtain information about the structure and dynamics of proteins and protein complexes. With the adv...
Nathaniel V Nucci,Bryan S Marques,Sabrina Bédard et al. Nathaniel V Nucci et al.
Comprehensive application of solution NMR spectroscopy to studies of macromolecules remains fundamentally limited by the molecular rotational correlation time. For proteins, molecules larger than 30 kDa require complex experimental methods,...
Jianglei Chen,Jianjun Wang Jianglei Chen
NMR structural determination of large multi-domain proteins is a challenging task due to significant spectral overlap with a particular difficulty in unambiguous identification of domain-domain interactions. Segmental labeling is a NMR stra...
Kan-Nian Hu,Wei Qiang,Robert Tycko Kan-Nian Hu
We describe a general computational approach to site-specific resonance assignments in multidimensional NMR studies of uniformly (15)N,(13)C-labeled biopolymers, based on a simple Monte Carlo/simulated annealing (MCSA) algorithm contained i...
Jianyang Zeng,Pei Zhou,Bruce Randall Donald Jianyang Zeng
One bottleneck in NMR structure determination lies in the laborious and time-consuming process of side-chain resonance and NOE assignments. Compared to the well-studied backbone resonance assignment problem, automated side-chain resonance a...
Yukiko Kamiya,Sayoko Yamamoto,Yasunori Chiba et al. Yukiko Kamiya et al.
This report describes a novel method for overexpression of (13)C-labeled oligosaccharides using genetically engineered Saccharomyces cerevisiae cells, in which a homogeneous high-mannose-type oligosaccharide accumulates because of deletions...