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nmr data analysis software bruker topspin  (Bruker Corporation)

 
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    Bruker Corporation nmr data analysis software bruker topspin
    Nmr Data Analysis Software Bruker Topspin, supplied by Bruker Corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/nmr+data+analysis+software+bruker+topspin/bruker+topspin+software/pmc11570622-235-6-11
    Average 90 stars, based on 1 article reviews
    nmr data analysis software bruker topspin - by Bioz Stars, 2026-10
    90/100 stars

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    Related Articles

    Nuclear Magnetic Resonance:

    Article Title: Discovery and biosynthesis of cyclic plant peptides via autocatalytic cyclases.
    Article Snippet: 1Department of Medicinal Chemistry, University of Michigan, Ann Arbor, MI, USA.. 2Bioinformatics Group, Wageningen University, Wageningen, Netherlands.. 3Natural Products Discovery Core, Life Sciences Institute, University of Michigan, Ann Arbor, MI, USA.

    Article Title: Tracking dendrites and solid electrolyte interphase formation with dynamic nuclear polarization—NMR spectroscopy
    Article Snippet: .. All NMR data analysis, deconvolution, and fitting were carried out using Bruker TopSpin and DMfit software . ..

    Software:

    Article Title: Tracking dendrites and solid electrolyte interphase formation with dynamic nuclear polarization—NMR spectroscopy
    Article Snippet: .. All NMR data analysis, deconvolution, and fitting were carried out using Bruker TopSpin and DMfit software . ..



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    A, two-dimensional 1H-1H trNOESY spectra of VG16KRKP–KYE28 complex in the LPS micelle, displaying the NOE contacts in the fingerprint region for CαH-NH and NH-NH resonances important for structure stabilization. B, parent peptide complex also displayed intra- and inter-molecular long-range NOE contacts, illustrating the importance of aromatic residues in the formation of a stabilized structure and justifying the strong synergistic interaction observed. The experiments were performed by titrating 0.6 mm of the total peptides with 10 μm LPS (LPS: each peptide = 1:30) at pH 4.5, using <t>a</t> <t>Bruker</t> Avance III 700 MHz <t>NMR</t> spectrometer (NOESY mixing time = 150 ms) and at 298 K (residues marked in blue are from VG16KKRP and in red are from KYE28).
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    A, two-dimensional 1H-1H trNOESY spectra of VG16KRKP–KYE28 complex in the LPS micelle, displaying the NOE contacts in the fingerprint region for CαH-NH and NH-NH resonances important for structure stabilization. B, parent peptide complex also displayed intra- and inter-molecular long-range NOE contacts, illustrating the importance of aromatic residues in the formation of a stabilized structure and justifying the strong synergistic interaction observed. The experiments were performed by titrating 0.6 mm of the total peptides with 10 μm LPS (LPS: each peptide = 1:30) at pH 4.5, using a Bruker Avance III 700 MHz NMR spectrometer (NOESY mixing time = 150 ms) and at 298 K (residues marked in blue are from VG16KKRP and in red are from KYE28).

    Journal: The Journal of Biological Chemistry

    Article Title: Structural insights into the combinatorial effects of antimicrobial peptides reveal a role of aromatic–aromatic interactions in antibacterial synergism

    doi: 10.1074/jbc.RA119.009955

    Figure Lengend Snippet: A, two-dimensional 1H-1H trNOESY spectra of VG16KRKP–KYE28 complex in the LPS micelle, displaying the NOE contacts in the fingerprint region for CαH-NH and NH-NH resonances important for structure stabilization. B, parent peptide complex also displayed intra- and inter-molecular long-range NOE contacts, illustrating the importance of aromatic residues in the formation of a stabilized structure and justifying the strong synergistic interaction observed. The experiments were performed by titrating 0.6 mm of the total peptides with 10 μm LPS (LPS: each peptide = 1:30) at pH 4.5, using a Bruker Avance III 700 MHz NMR spectrometer (NOESY mixing time = 150 ms) and at 298 K (residues marked in blue are from VG16KKRP and in red are from KYE28).

    Article Snippet: NMR data were analyzed using Bruker TOPSPIN TM 3.1 and SPARKY ( 85 ).

    Techniques:

    A, two-dimensional 1H-1H trNOESY spectra of VG16KRKP–KYE28 in a 3:1 POPE/POPG vesicle, displaying the NOE contacts in the fingerprint region for CαH-NH and NH-NH resonances important for structure stabilization. VG16KRKP–KYE28 upon interaction with 3:1 POPE/POPG vesicles exhibited several trNOEs hinting toward the adoption of a rigid and well-converged structure. B, parent peptide complex, also displayed intra- and inter-molecular long-range NOE contacts. The experiments were performed by titrating 0.6 mm of the total peptides with 12 μm of 3:1 POPE/POPG LUV (LUV: each peptide = 1:25) at pH 4.5, using a Bruker Avance III 700 MHz NMR spectrometer (NOESY mixing time = 150 ms) and at 298 K (residues marked in blue are from VG16KKRP and in red from KYE28).

    Journal: The Journal of Biological Chemistry

    Article Title: Structural insights into the combinatorial effects of antimicrobial peptides reveal a role of aromatic–aromatic interactions in antibacterial synergism

    doi: 10.1074/jbc.RA119.009955

    Figure Lengend Snippet: A, two-dimensional 1H-1H trNOESY spectra of VG16KRKP–KYE28 in a 3:1 POPE/POPG vesicle, displaying the NOE contacts in the fingerprint region for CαH-NH and NH-NH resonances important for structure stabilization. VG16KRKP–KYE28 upon interaction with 3:1 POPE/POPG vesicles exhibited several trNOEs hinting toward the adoption of a rigid and well-converged structure. B, parent peptide complex, also displayed intra- and inter-molecular long-range NOE contacts. The experiments were performed by titrating 0.6 mm of the total peptides with 12 μm of 3:1 POPE/POPG LUV (LUV: each peptide = 1:25) at pH 4.5, using a Bruker Avance III 700 MHz NMR spectrometer (NOESY mixing time = 150 ms) and at 298 K (residues marked in blue are from VG16KKRP and in red from KYE28).

    Article Snippet: NMR data were analyzed using Bruker TOPSPIN TM 3.1 and SPARKY ( 85 ).

    Techniques: