Journal: Journal of Biomolecular NMR

Abbreviation

J Biomol NMR

Publisher

Springer

Journal Volumes

ISSN

0925-2738
1573-5001

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Publications 1 - 10 of 123
  • Automatic assignment of protein backbone resonances by direct spectrum inspection in targeted acquisition of NMR data
    Item type: Journal Article
    Wong, Leo E.; Masse, James E.; Jaravine, Victor; et al. (2008)
    Journal of Biomolecular NMR
  • Site-specific analysis of heteronuclear Overhauser effects in microcrystalline proteins
    Item type: Journal Article
    Amo, Juan Miguel Lopez Del; Agarwal, Vipin Kumar; Sarkar, Riddhiman; et al. (2014)
    Journal of Biomolecular NMR
  • The NMR signature of gluconoylation: a frequent N-terminal modification of isotope-labeled proteins
    Item type: Journal Article
    Schweida, David; Barraud, Pierre; Regl, Christof; et al. (2019)
    Journal of Biomolecular NMR
    N-terminal gluconoylation is a moderately widespread modification in recombinant proteins expressed in Escherichia coli, in particular in proteins bearing an N-terminal histidine-tag. This post-translational modification has been investigated mainly by mass spectrometry. Although its NMR signals must have been observed earlier in spectra of 13C/15N labeled proteins, their chemical shifts were not yet reported. Here we present the complete 1H and 13C chemical shift assignment of the N-terminal gluconoyl post-translational modification, based on a selection of His-tagged protein constructs (CCL2, hnRNP A1 and Lin28) starting with Met-Gly-...-(His)6. In addition, we show that the modification can hydrolyze over time, resulting in a free N-terminus and gluconate. This leads to the disappearance of the gluconoyl signals and the appearance of gluconate signals during the NMR measurements. The chemical shifts presented here can now be used as a reference for the identification of gluconoylation in recombinant proteins, in particular when isotopically labeled.
  • Solid-state NMR spectroscopy of 10% 13C labeled ubiquitin
    Item type: Journal Article
    Schubert, Mario; Manolikas, Theofanis; Rogowski, Marco; et al. (2006)
    Journal of Biomolecular NMR
  • The J-UNIO protocol for automated protein structure determination by NMR in solution
    Item type: Journal Article
    Serrano, Pedro; Pedrini, Bill; Mohanty, Biswaranjan; et al. (2012)
    Journal of Biomolecular NMR
  • Solution NMR structure determination of proteins revisited
    Item type: Journal Article
    Billeter, Martin; Wagner, Gerhard; Wuethrich, Kurt (2008)
    Journal of Biomolecular NMR
  • Fluorine-19 labeling of the tryptophan residues in the G proteincoupled receptor NK1R using the 5-fluoroindole precursor in Pichia pastoris expression
    Item type: Journal Article
    Pan, Benxun; Guo, Canyong; Liu, Dongsheng; et al. (2024)
    Journal of Biomolecular NMR
    In NMR spectroscopy of biomolecular systems, the use of fluorine-19 probes benefits from a clean background and high sensitivity. Therefore, F-19-labeling procedures are of wide-spread interest. Here, we use 5-fluoroindole as a precursor for cost-effective residue-specific introduction of 5-fluorotryptophan (5F-Trp) into G protein-coupled receptors (GPCRs) expressed in Pichia pastoris. The method was successfully implemented with the neurokinin 1 receptor (NK1R). The F-19-NMR spectra of 5F-Trp-labeled NK1R showed one well-separated high field-shifted resonance, which was assigned by mutational studies to the "toggle switch tryptophan". Residue-selective labeling thus enables site-specific investigations of this functionally important residue. The method described here is inexpensive, requires minimal genetic manipulation and can be expected to be applicable for yeast expression of GPCRs at large.
  • NMR studies of structure and function of biological macromolecules (Nobel Lecture)
    Item type: Journal Article
    Wüthrich, Kurt (2003)
    Journal of Biomolecular NMR
  • Time-averaged order parameter restraints in molecular dynamics simulations
    Item type: Journal Article
    Hansen, Niels; Heller, Fabian; Schmid, Nathan; et al. (2014)
    Journal of Biomolecular NMR
    A method is described that allows experimental S2 order parameters to be enforced as a time-averaged quantity in molecular dynamics simulations. The two parameters that characterize time-averaged restraining, the memory relaxation time and the weight of the restraining potential energy term in the potential energy function used in the simulation, are systematically investigated based on two model systems, a vector with one end restrained in space and a pentapeptide. For the latter it is shown that the backbone N–H order parameter of individual residues can be enforced such that the spatial fluctuations of quantities depending on atomic coordinates are not significantly perturbed. The applicability to realistic systems is illustrated for the B3 domain of protein G in aqueous solution.
  • Properties of the DREAM scheme and its optimization for application to proteins
    Item type: Journal Article
    Westfeld, Thomas; Verel, René; Ernst, Matthias; et al. (2012)
    Journal of Biomolecular NMR
Publications 1 - 10 of 123