Journal of Biomolecular NMR

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Amino–acid-type selective isotope labeling of proteins expressed in Baculovirus-infected insect cells useful for NMR studies
Journal of Biomolecular NMR - Tập 26 - Trang 367-372 - 2003
André Strauss, Francis Bitsch, Brian Cutting, Gabriele Fendrich, Patrick Graff, Janis Liebetanz, Mauro Zurini, Wolfgang Jahnke
Culture conditions for successful amino–acid-type selective isotope labeling of proteins expressed in Baculovirus-infected insect cells are described. The method was applied to the selective labeling of the catalytic domain of c-Abl kinase with 15N-phenylalanine, 15N-glycine, 15N-tyrosine or 15N-valine. For the essential amino acids phenylalanine, tyrosine and valine high 15N-label incorporation r...... hiện toàn bộ
Determination of methyl order parameters using solid state NMR under off magic angle spinning
Journal of Biomolecular NMR - Tập 73 - Trang 471-475 - 2019
Kai Xue, Salvatore Mamone, Benita Koch, Riddhiman Sarkar, Bernd Reif
Quantification of dipolar couplings in biological solids is important for the understanding of dynamic processes. Under Magic Angle Spinning (MAS), order parameters are normally obtained by recoupling of anisotropic interactions involving the application of radio frequency pulses. We have recently shown that amide backbone order parameters can be estimated accurately in a spin-echo experiment in c...... hiện toàn bộ
Letter to the Editor:1H,13C and15N resonance assignments for the N-cadherin prodomain
Journal of Biomolecular NMR - Tập 28 Số 1 - Trang 87-88 - 2004
Alexander W. Koch, Amjad Farooq, Lei Zeng, David Colman, Ming Zhou
Heteronuclear relayed E.COSY applied to the determination of accurate 3J(HN,C′) and 3J(Hβ,C′) coupling constants in Desulfovibrio vulgaris flavodoxin
Journal of Biomolecular NMR - - 1996
Jürgen M. Schmidt, Frank Löhr, Heinz Rüterjans
A simple constant-time 3D heteronuclear NMR pulse sequence has been developed to quantitatively determine the heteronuclear three-bond couplings 3J(HN,C′) and 3J(Hβ,C′) in uniformly 13C-enriched proteins. The protocols for measuring accurate coupling constants are based on 1H,13C-heteronuclear relayed E.COSY [Schmidt, J.M., Ernst, R.R., Aimoto, S. and Kainosho, M. (1995) J. Biomol. NMR, 6, 95–105]...... hiện toàn bộ
Myristoylation as a general method for immobilization and alignment of soluble proteins for solid-state NMR structural studies
Journal of Biomolecular NMR - Tập 25 - Trang 55-61 - 2003
M.F. Mesleh, K.G. Valentine, S.J. Opella, J.M. Louis, A.M. Gronenborn
N-terminal myristoylation of the immunoglobulin-binding domain of protein G (GB1) from group G Streptococcus provides the means to bind the protein to aligned phospholipid bilayers for solid-state NMR structural studies. The myristoylated protein is immobilized by its interactions with bilayers, and the sample alignment enables orientationally dependent 15N chemical shifts and 1H-15N-dipolar coupl...... hiện toàn bộ
A general Bayesian method for an automated signal class recognition in 2D NMR spectra combined with a multivariate discriminant analysis
Journal of Biomolecular NMR - - 1995
C. Antz, Klaus−Peter Neidig, Hans Robert Kalbitzer
1H, 13C and 15N NMR backbone assignments of 25.5 kDa metallo-β-lactamase from shape Bacteroides fragilis
Journal of Biomolecular NMR - Tập 12 - Trang 201-202 - 1998
Sergio D.B. Scrofani, Peter E. Wright, H. Jane Dyson
[2-3H]ATP synthesis and 3H NMR spectroscopy of enzyme-nucleotide complexes: ADP and ADP.Vi bound to myosin subfragment 1
Journal of Biomolecular NMR - Tập 3 - Trang 325-334 - 1993
Stefan Highsmith, Mark Kubinec, Devendra K. Jaiswal, Hiromi Morimoto, Philip G. Williams, David E. Wemmer
The synthesis of [2-3H]ATP with specific activity high enough to use for 3H NMR spectroscopy at micromolar concentrations was accomplished by tritiodehalogenation of 2-Br-ATP. ATP with greater than 80% substitution at the 2-position and negligible tritium levels at other positions had a single 3H NMR peak at 8.20 ppm in 1D spectra obtained at 533 MHz. This result enables the application of tritium...... hiện toàn bộ
Combination of 15N reverse labeling and afterglow spectroscopy for assigning membrane protein spectra by magic-angle-spinning solid-state NMR: application to the multidrug resistance protein EmrE
Journal of Biomolecular NMR - Tập 55 - Trang 391-399 - 2013
James R. Banigan, Anindita Gayen, Nathaniel J. Traaseth
Magic-angle-spinning (MAS) solid-state NMR spectroscopy has emerged as a viable method to characterize membrane protein structure and dynamics. Nevertheless, the spectral resolution for uniformly labeled samples is often compromised by redundancy of the primary sequence and the presence of helical secondary structure that results in substantial resonance overlap. The ability to simplify the spectr...... hiện toàn bộ
Erratum to: Correlation of chemical shifts predicted by molecular dynamics simulations for partially disordered proteins
Journal of Biomolecular NMR - Tập 62 - Trang 119-119 - 2015
Jerome M. Karp, Ertan Eryilmaz, David Cowburn
Tổng số: 2,215   
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