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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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Eriks Kupče,Lewis E Kay Eriks Kupče
We introduce the use of multiple receivers applied in parallel for simultaneously recording multi-dimensional data sets of proteins in a single experiment. The utility of the approach is established through the introduction of the 2D (15)N,...
Garima Jaipuria,Nitin Prakash Lobo,Divya Shet et al. Garima Jaipuria et al.
New ¹³C-detected NMR experiments have been devised for molecules in solution and solid state, which provide chemical shift correlations of methyl groups with high resolution, selectivity and sensitivity. The experiments achieve selective ...
Ulrich Weininger,Carl Diehl,Mikael Akke Ulrich Weininger
Aromatic side chains are prevalent in protein binding sites, perform functional roles in enzymatic catalysis, and form an integral part of the hydrophobic core of proteins. Thus, it is of great interest to probe the conformational dynamics ...
Pedro Serrano,Bill Pedrini,Biswaranjan Mohanty et al. Pedro Serrano et al.
The J-UNIO (JCSG protocol using the software UNIO) procedure for automated protein structure determination by NMR in solution is introduced. In the present implementation, J-UNIO makes use of APSY-NMR spectroscopy, 3D heteronuclear-resolved...
Yuichi Minato,Takumi Ueda,Asako Machiyama et al. Yuichi Minato et al.
Segmental isotopic labeling is a powerful labeling tool to facilitate NMR studies of larger proteins by not only alleviating the signal overlap problem but also retaining features of uniform isotopic labeling. Although two approaches, expre...
Rinaldo W Montalvao,Alfonso De Simone,Michele Vendruscolo Rinaldo W Montalvao
Residual dipolar couplings (RDCs) have the potential of providing detailed information about the conformational fluctuations of proteins. It is very challenging, however, to extract such information because of the complex relationship betwe...
Niel M Henriksen,Darrell R Davis,Thomas E Cheatham rd Niel M Henriksen
Restrained molecular dynamics simulations are a robust, though perhaps underused, tool for the end-stage refinement of biomolecular structures. We demonstrate their utility-using modern simulation protocols, optimized force fields, and incl...
Denise Steiner,Jane R Allison,Andreas P Eichenberger et al. Denise Steiner et al.
Structural knowledge about proteins is mainly derived from values of observables, measurable in NMR spectroscopic or X-ray diffraction experiments, i.e. absorbed or scattered intensities, through theoretically derived relationships between ...