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  • 1. Brun, E.
    et al.
    Brumer, Harry
    KTH, Tidigare Institutioner                               , Bioteknologi.
    MacKenzie, L. F.
    Withers, S. G.
    McIntosh, L. P.
    Letter to the Editor: Assignment of selectively C-13-labeled cellopentaose synthesized using an engineered glycosynthase2001Inngår i: Journal of Biomolecular NMR, ISSN 0925-2738, E-ISSN 1573-5001, Vol. 21, nr 1, s. 67-68Artikkel i tidsskrift (Fagfellevurdert)
  • 2.
    Dogan, Jakob
    et al.
    KTH, Skolan för bioteknologi (BIO).
    Lendel, Christofer
    KTH, Skolan för bioteknologi (BIO).
    Härd, Torleif
    Göteborgs Universitet.
    NMR assignments of the free and bound-state protein components of an anti-idiotypic affibody complex2006Inngår i: Journal of Biomolecular NMR, ISSN 0925-2738, E-ISSN 1573-5001, Vol. 36, s. (Electronic publication ahead of print Feb. 6; doi:10.1007/s10858-005-5350-8)Artikkel i tidsskrift (Fagfellevurdert)
  • 3. Helgstrand, M
    et al.
    Allard, Peter
    KTH, Tidigare Institutioner, Bioteknologi.
    QSim, a program for NMR simulations2004Inngår i: Journal of Biomolecular NMR, ISSN 0925-2738, E-ISSN 1573-5001, Vol. 30, nr 1, s. 71-80Artikkel i tidsskrift (Fagfellevurdert)
    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, Tidigare Institutioner, Bioteknologi.
    Li, Y C
    Jendeberg, Lena
    KTH, Tidigare Institutioner, Bioteknologi.
    Anderson, S
    Montelione, B T
    Nilsson, B
    High-level production of uniformly 15N- and 13C-enriched fusion proteins in Escherichia coli.1996Inngår i: Journal of Biomolecular NMR, ISSN 0925-2738, E-ISSN 1573-5001, Vol. 7, nr 2, s. 131-41Artikkel i tidsskrift (Fagfellevurdert)
    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, Tidigare Institutioner                               , Bioteknologi.
    Wahlberg, Elisabet
    KTH, Tidigare Institutioner                               , Bioteknologi.
    Berglund, Helena
    KTH, Tidigare Institutioner                               , Bioteknologi.
    Eklund, Malin
    KTH, Tidigare Institutioner                               , Bioteknologi.
    Nygren, Per-Åke
    KTH, Tidigare Institutioner                               , Bioteknologi.
    Härd, Torleif
    KTH, Tidigare Institutioner                               , Bioteknologi.
    1H, 13C and 15N resonance assignments of an affibody-target complex2002Inngår i: Journal of Biomolecular NMR, ISSN 0925-2738, E-ISSN 1573-5001, Vol. 24, nr 3, s. 271-272Artikkel i tidsskrift (Fagfellevurdert)
  • 6.
    Woestenenk, Esmeralda A.
    et al.
    KTH, Tidigare Institutioner, Bioteknologi.
    Allard, Peter
    KTH, Tidigare Institutioner, Bioteknologi.
    Gongadze, G. M.
    Moskalenko, S. E.
    Shcherbakov, D. V.
    Rak, A. V.
    Garber, M B
    Härd, Torleif
    KTH, Tidigare Institutioner, Bioteknologi.
    Berglund, Helena
    KTH, Tidigare Institutioner, Bioteknologi.
    Assignment and secondary structure identification of the ribosomal protein L18 from Thermus thermophilus2000Inngår i: Journal of Biomolecular NMR, ISSN 0925-2738, E-ISSN 1573-5001, Vol. 17, nr 3, s. 273-274Artikkel i tidsskrift (Fagfellevurdert)
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