Journal of Biomolecular NMR

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Accurate measurement of 3JHNHα couplings in small or disordered proteins from WATERGATE-optimized TROSY spectra
Journal of Biomolecular NMR - Tập 64 - Trang 1-7 - 2015
Julien Roche, Jinfa Ying, Ad Bax
Provided that care is taken in adjusting the WATERGATE element of a 1H–15N TROSY-HSQC experiment, such that neither the water magnetization nor the 1Hα protons are inverted by its final 180° pulse, 3JHNHα couplings can be measured directly from splittings in the 1H dimension of the spectrum. With band-selective 1H decoupling, very high 15N resolution can be achieved. A complete set of 3JHNHα value... hiện toàn bộ
Time-shared HSQC-NOESY for accurate distance constraints measured at high-field in 15N-13C-ILV methyl labeled proteins
Journal of Biomolecular NMR - Tập 45 Số 3 - Trang 311-318 - 2009
Dominique P. Frueh, Alison Leed, Haribabu Arthanari, Alexander Koglin, Christopher T. Walsh, Gerhard Wagner
1H and 15N NMR assignment and solution structure of the SH3 domain of spectrin: Comparison of unrefined and refined structure sets with the crystal structure
Journal of Biomolecular NMR - Tập 9 - Trang 347-357 - 1997
Francisco J. Blanco, Ángel R. Ortiz, Luis Serrano
The assignment of the 1H and 15Nnuclear magnetic resonance spectra of the Src-homology region 3 domain ofchicken brain α-spectrin has been obtained. A set of solutionstructures has been determined from distance and dihedral angle restraints,which provide a reasonable representation of the protein structure insolution, as evaluated by a principal component analysis of the globalpairwise root-mean-s... hiện toàn bộ
Letter to the Editor: 1H, 13C, 15N backbone and sidechain resonance assignments of apo-NosL, a novel copper(I) binding protein from the nitrous oxide reductase gene cluster of Achromobacter cycloclastes
Journal of Biomolecular NMR - Tập 29 - Trang 211-212 - 2004
Lara M. Taubner, Michele A. McGuirl, David M. Dooley, Valérie Copié
1H and 15N NMR resonance assignments and secondary structure of titin type I domains
Journal of Biomolecular NMR - Tập 9 - Trang 2-10 - 1997
Claudia Muhle-Goll, Michael Nilges, Annalisa Pastore
Titin/connectin is a giant muscle protein with a highly modular architecture consisting ofmultiple repeats of two sequence motifs, named type I and type II. Type I modules have beensuggested to be intracellular members of the fibronectin type III (Fn3) domain family. Alongthe titin sequence they are exclusively present in the region of the molecule located in thesarcomere A-band. This region has b... hiện toàn bộ
Compressed sensing reconstruction of undersampled 3D NOESY spectra: application to large membrane proteins
Journal of Biomolecular NMR - Tập 54 - Trang 15-32 - 2012
Mark J. Bostock, Daniel J. Holland, Daniel Nietlispach
Central to structural studies of biomolecules are multidimensional experiments. These are lengthy to record due to the requirement to sample the full Nyquist grid. Time savings can be achieved through undersampling the indirectly-detected dimensions combined with non-Fourier Transform (FT) processing, provided the experimental signal-to-noise ratio is sufficient. Alternatively, resolution and sign... hiện toàn bộ
Letter to the Editor: Sequence-specific chemical shift assignment and chemical shift indexing of murine apo-Mts1
Journal of Biomolecular NMR - Tập 22 - Trang 181-182 - 2002
Kaushik Dutta, Cathleen J. Cox, Andrei Alexandrov, He Huang, Ravi Basavappa, Steven M. Pascal
Correction of the NMR structure of the ETS1/DNA complex
Journal of Biomolecular NMR - Tập 10 - Trang 317-328 - 1997
Milton H. Werner, G. Marius Clore, Constance L. Fisher, Robert J. Fisher, Loc Trinh, Joseph Shiloach, Angela M. Gronenborn
The ETS family of transcription factors consists of a group of proteins that share a highly conserved 85 amino acid DNA-binding domain (DBD). This family recognizes a consensus sequence rich in purine bases with a central GGAA motif. A comparison of the published three-dimensional structures of the DBD/DNA complexes of ETS1 by NMR [Werner et al. (1995) Cell, 83, 761–771] and the related Pu.1 by X-... hiện toàn bộ
Single Transition-to-single Transition Polarization Transfer (ST2-PT) in [15N,1H]-TROSY
Journal of Biomolecular NMR - Tập 12 - Trang 345-348 - 1998
Konstantin V. Pervushin, Gerhard Wider, Kurt Wüthrich
This paper describes the use of single transition-to-single transition polarization transfer (ST2-PT) in transverse relaxation-optimized spectroscopy (TROSY), where it affords a $$\sqrt 2$$ sensitivity enhancement for kinetically stable amide 15N-1H groups in proteins. Additional, conventional improvements of [15N,1H]-TROSY include that signal loss for kinetically labile 15N-1H groups due to satur... hiện toàn bộ
A non-uniform sampling approach enables studies of dilute and unstable proteins
Journal of Biomolecular NMR - Tập 68 - Trang 119-127 - 2017
Tomas Miljenović, Xinying Jia, Peter Lavrencic, Bostjan Kobe, Mehdi Mobli
NMR spectroscopy is a powerful method in structural and functional analysis of macromolecules and has become particularly prevalent in studies of protein structure, function and dynamics. Unique to NMR spectroscopy is the relatively low constraints on sample preparation and the high level of control of sample conditions. Proteins can be studied in a wide range of buffer conditions, e.g. different ... hiện toàn bộ
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