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  • 1. Brun, E.
    et al.
    Brumer, Harry
    KTH, Superseded Departments, Biotechnology.
    MacKenzie, L. F.
    Withers, S. G.
    McIntosh, L. P.
    Letter to the Editor: Assignment of selectively C-13-labeled cellopentaose synthesized using an engineered glycosynthase2001In: Journal of Biomolecular NMR, ISSN 0925-2738, E-ISSN 1573-5001, Vol. 21, no 1, p. 67-68Article in journal (Refereed)
  • 2.
    Dogan, Jakob
    et al.
    KTH, School of Biotechnology (BIO).
    Lendel, Christofer
    KTH, School of Biotechnology (BIO).
    Härd, Torleif
    Göteborgs Universitet.
    NMR assignments of the free and bound-state protein components of an anti-idiotypic affibody complex2006In: Journal of Biomolecular NMR, ISSN 0925-2738, E-ISSN 1573-5001, Vol. 36, p. (Electronic publication ahead of print Feb. 6; doi:10.1007/s10858-005-5350-8)Article in journal (Refereed)
  • 3. Helgstrand, M
    et al.
    Allard, Peter
    KTH, Superseded Departments, Biotechnology.
    QSim, a program for NMR simulations2004In: Journal of Biomolecular NMR, ISSN 0925-2738, E-ISSN 1573-5001, Vol. 30, no 1, p. 71-80Article in journal (Refereed)
    Abstract [en]

    We present QSim, a program for simulation of NMR experiments. Pulse sequences are implemented and analyzed in QSim using a mouse driven interface. QSim can handle almost any modern NMR experiment, using multiple channels, shaped pulses, mixing, decoupling, phase-cycling and pulsed field gradients. Any number of spins with any spin quantum number can, in theory, be used in simulations. Relaxation is accounted for during all steps of pulse sequences and relaxation interference effects are supported. Chemical kinetics between any numbers of states can be simulated. Both classical and quantum mechanical calculations can be performed. The result of a simulation can be presented either as magnetization as a function of time or as a processed spectrum.

  • 4.
    Jansson, Magnus
    et al.
    KTH, Superseded Departments, Biotechnology.
    Li, Y C
    Jendeberg, Lena
    KTH, Superseded Departments, Biotechnology.
    Anderson, S
    Montelione, B T
    Nilsson, B
    High-level production of uniformly 15N- and 13C-enriched fusion proteins in Escherichia coli.1996In: Journal of Biomolecular NMR, ISSN 0925-2738, E-ISSN 1573-5001, Vol. 7, no 2, p. 131-41Article in journal (Refereed)
    Abstract [en]

    An approach to produce 13C- and 15N-enriched proteins is described. The concept is based on intracellular production of the recombinant proteins in Escherichia coli as fusions to an IgG-binding domain, Z, derived from staphylococcal protein A. The production method provides yields of 40-200 mg/l of isotope-enriched fusion proteins in defined minimal media. In addition, the Z fusion partner facilitates the first purification step by IgG affinity chromatography. The production system is applied to isotope enrichment of human insulin-like growth factor II (IGF-II), bovine pancreatic trypsin inhibitor (BPTI), and Z itself. High levels of protein production are achieved in shaker flasks using totally defined minimal medium supplemented with 13C(6)-glucose and (15NH4)2SO4 as the only carbon and nitrogen sources. Growth conditions were optimized to obtain high protein production levels and high levels of isotope incorporation, while minimizing 13C(6)-glucose usage. Incorporation levels of 13C and/or 15N isotopes in purifies IGF-II, BPTI, and Z were confirmed using mass spectrometry and NMR spectroscopy. More than 99% of total isotope enrichment was obtained using a defined isotope-enriched minimal medium. The optimized systems provide reliable, high-level production of isotope-enriched fusion proteins. They can be used to produce 20-40 mg/l of properly folded Z and BPTI proteins. The production system of recombinant BPTI is state-of-the-art and provides the highest known yield of native refolded BPTI.

  • 5.
    Lendel, Christofer
    et al.
    KTH, Superseded Departments, Biotechnology.
    Wahlberg, Elisabet
    KTH, Superseded Departments, Biotechnology.
    Berglund, Helena
    KTH, Superseded Departments, Biotechnology.
    Eklund, Malin
    KTH, Superseded Departments, Biotechnology.
    Nygren, Per-Åke
    KTH, Superseded Departments, Biotechnology.
    Härd, Torleif
    KTH, Superseded Departments, Biotechnology.
    1H, 13C and 15N resonance assignments of an affibody-target complex2002In: Journal of Biomolecular NMR, ISSN 0925-2738, E-ISSN 1573-5001, Vol. 24, no 3, p. 271-272Article in journal (Refereed)
  • 6.
    Woestenenk, Esmeralda A.
    et al.
    KTH, Superseded Departments, Biotechnology.
    Allard, Peter
    KTH, Superseded Departments, Biotechnology.
    Gongadze, G. M.
    Moskalenko, S. E.
    Shcherbakov, D. V.
    Rak, A. V.
    Garber, M B
    Härd, Torleif
    KTH, Superseded Departments, Biotechnology.
    Berglund, Helena
    KTH, Superseded Departments, Biotechnology.
    Assignment and secondary structure identification of the ribosomal protein L18 from Thermus thermophilus2000In: Journal of Biomolecular NMR, ISSN 0925-2738, E-ISSN 1573-5001, Vol. 17, no 3, p. 273-274Article in journal (Refereed)
1 - 6 of 6
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