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Bruker Corporation bruker avance 400
Bruker Avance 400, supplied by Bruker Corporation, used in various techniques. Bioz Stars score: 97/100, based on 40 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 97 stars, based on 40 article reviews
Price from $9.99 to $1999.99
bruker avance 400 - by Bioz Stars, 2022-09
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    Bruker Corporation pulsed nmr spectrometer
    1 H <t>MAS</t> <t>NMR</t> spectra for the samples (a) before and (b) after irradiation at 430 K following various spin-locking pulse lengths. Vertical arrows denote the peaks at 1.0 (H1) and 1.4 ppm (H2) before irradiation, as well as those and 4.1 ppm (H3) after irradiation. Inset shows the spectra before and after irradiation following a spin-locking pulse of 0.1 ms for comparison.
    Pulsed Nmr Spectrometer, supplied by Bruker Corporation, used in various techniques. Bioz Stars score: 95/100, based on 83 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pulsed nmr spectrometer/product/Bruker Corporation
    Average 95 stars, based on 83 article reviews
    Price from $9.99 to $1999.99
    pulsed nmr spectrometer - by Bioz Stars, 2022-09
    95/100 stars
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    90
    Bruker Corporation avance neo 400 mhz nmr spectrometer
    (i) Integrated normalized polymer signals in the range of δ = 1–3 ppm as acquired in temperature-dependent 1 <t>H-NMR</t> spectra (circles; left and bottom axis, integrals are normalized on the lowest temperature) and (ii) extracted VPTTs (squares; right and top axis) for neat microgels containing different crosslinker content. Color code as indicated in the legend. Dashed line is guide to the eye. Solid lines are fits according to Equation (4).
    Avance Neo 400 Mhz Nmr Spectrometer, 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/result/avance neo 400 mhz nmr spectrometer/product/Bruker Corporation
    Average 90 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    avance neo 400 mhz nmr spectrometer - by Bioz Stars, 2022-09
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    91
    Bruker Corporation avance neo 400 nmr spectrometer
    Partial atom connectivity map of 4c derived from 2D <t>NMR</t> data.
    Avance Neo 400 Nmr Spectrometer, supplied by Bruker Corporation, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/avance neo 400 nmr spectrometer/product/Bruker Corporation
    Average 91 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    avance neo 400 nmr spectrometer - by Bioz Stars, 2022-09
    91/100 stars
      Buy from Supplier

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    1 H MAS NMR spectra for the samples (a) before and (b) after irradiation at 430 K following various spin-locking pulse lengths. Vertical arrows denote the peaks at 1.0 (H1) and 1.4 ppm (H2) before irradiation, as well as those and 4.1 ppm (H3) after irradiation. Inset shows the spectra before and after irradiation following a spin-locking pulse of 0.1 ms for comparison.

    Journal: Scientific Reports

    Article Title: NMR Observation of Mobile Protons in Proton-Implanted ZnO Nanorods

    doi: 10.1038/srep23378

    Figure Lengend Snippet: 1 H MAS NMR spectra for the samples (a) before and (b) after irradiation at 430 K following various spin-locking pulse lengths. Vertical arrows denote the peaks at 1.0 (H1) and 1.4 ppm (H2) before irradiation, as well as those and 4.1 ppm (H3) after irradiation. Inset shows the spectra before and after irradiation following a spin-locking pulse of 0.1 ms for comparison.

    Article Snippet: The 1 H magic-angle spinning (MAS) NMR measurements were made by using a 400-MHz 1 H pulsed NMR spectrometer (Bruker Avance II+ ) with a spinning rate of 7 kHz.

    Techniques: Nuclear Magnetic Resonance, Irradiation, Mass Spectrometry

    1 H MAS NMR spectra for the samples (a) before and (b) after irradiation at various temperatures. The H1 and H2 represent the resonance lines at 1.0 and 1.4 ppm before and after irradiation, respectively. A broad resonance line before irradiation is denoted by H0, which is shifted upfield with increasing temperature. The resonance line at 4.1 ppm after irradiation is denoted by H3.

    Journal: Scientific Reports

    Article Title: NMR Observation of Mobile Protons in Proton-Implanted ZnO Nanorods

    doi: 10.1038/srep23378

    Figure Lengend Snippet: 1 H MAS NMR spectra for the samples (a) before and (b) after irradiation at various temperatures. The H1 and H2 represent the resonance lines at 1.0 and 1.4 ppm before and after irradiation, respectively. A broad resonance line before irradiation is denoted by H0, which is shifted upfield with increasing temperature. The resonance line at 4.1 ppm after irradiation is denoted by H3.

    Article Snippet: The 1 H magic-angle spinning (MAS) NMR measurements were made by using a 400-MHz 1 H pulsed NMR spectrometer (Bruker Avance II+ ) with a spinning rate of 7 kHz.

    Techniques: Nuclear Magnetic Resonance, Irradiation

    Verification of purified recombinant PanD proteins and effect of POA on PanD enzymatic activity. a Schematic depicting the autocleavage of PanD at the Gly24-Ser25 position to yield enzymatically active enzyme comprising of a C-terminal (PanD-α) and an N-terminal fragment (PanD-β) 15 . b Twelve percent SDS-PAGE of purified, N-terminal His-tagged recombinant proteins PanD WT (WT) and C-terminal truncated, non-POA binding PanD 127TRASC131 (TRASC). To determine the identity of the protein bands, the bands corresponding to P1, P2, and P3 were cut out, in-gel digested with trypsin and subjected to LC–MS analysis. PanD is synthesized as a proenzyme and rapidly autocatalytically cleaved at its N-terminus, resulting in a small N-terminal fragment (P3, expected size including His Tag for WT and TRASC: 3.75 kDa) and a larger C-terminal polypeptide (P2, expected size for WT: 12.15 kDa and TRASC: 11.4 kDa). Traces of uncleaved proenzyme are indicated (P1, expected size including His Tag for WT: 15.9 kDa and TRASC: 15.15 kDa). Black and red arrows indicate the corresponding protein bands of wild-type and truncated PanD, respectively. c , d Time-dependent conversion of L-Aspartate (2 mM) to β-Alanine (β-Ala) as determined by 1 H NMR after addition of 10 µM Mtb PanD WT in D 2 O at 298 K on a Bruker Avance 400 MHz spectrometer. Shown are ( c ) representative 1 H NMR spectra and ( d ) a plot of time-dependent β-Alanine formation at different incubation times by measuring the peak volume of converted L-Asp to β-Ala. At t = 40 min, ~50% conversion of L-aspartate to β-Alanine was observed as determined by integration of peak values. Thus, 40 min was chosen as a reference point within the linear range of PanD enzyme kinetics for subsequent enzyme assays. e Effect of POA on the formation of β-Ala by recombinant PanD WT and POA-resistant PanD 127TRASC131 proteins, respectively, as determined by 1 H NMR. The plot shows the results of a representative experiment. NMR spectra for e are shown in Supplementary Fig. 1 . Both recombinant proteins were purified as described 4 . The NMR experiments were repeated twice independently, yielding the same results. The results from a representative experiment are shown. Error bars were defined as 5% standard deviations. Source data are provided as a Source Data file. The cleaved form of the wild-type protein P2 migrates as a doublet with similar staining intensity. The reason for this behavior remains to be determined. LC–MS analysis of the doublet band suggests that both sub-bands present P2 (Supplementary Data 1 _P123seq). The P2 doublet is specific to recombinant wild-type protein and is not observed in the mutant PanD 127TRASC131 or in whole cell extracts (see Fig. 4 , western blot analyses). The SDS-PAGE analyses show that the recombinant PanD protein preparations used for in vitro analyses in the current study presented largely the cleaved, active form of the enzyme.

    Journal: Nature Communications

    Article Title: Pyrazinamide triggers degradation of its target aspartate decarboxylase

    doi: 10.1038/s41467-020-15516-1

    Figure Lengend Snippet: Verification of purified recombinant PanD proteins and effect of POA on PanD enzymatic activity. a Schematic depicting the autocleavage of PanD at the Gly24-Ser25 position to yield enzymatically active enzyme comprising of a C-terminal (PanD-α) and an N-terminal fragment (PanD-β) 15 . b Twelve percent SDS-PAGE of purified, N-terminal His-tagged recombinant proteins PanD WT (WT) and C-terminal truncated, non-POA binding PanD 127TRASC131 (TRASC). To determine the identity of the protein bands, the bands corresponding to P1, P2, and P3 were cut out, in-gel digested with trypsin and subjected to LC–MS analysis. PanD is synthesized as a proenzyme and rapidly autocatalytically cleaved at its N-terminus, resulting in a small N-terminal fragment (P3, expected size including His Tag for WT and TRASC: 3.75 kDa) and a larger C-terminal polypeptide (P2, expected size for WT: 12.15 kDa and TRASC: 11.4 kDa). Traces of uncleaved proenzyme are indicated (P1, expected size including His Tag for WT: 15.9 kDa and TRASC: 15.15 kDa). Black and red arrows indicate the corresponding protein bands of wild-type and truncated PanD, respectively. c , d Time-dependent conversion of L-Aspartate (2 mM) to β-Alanine (β-Ala) as determined by 1 H NMR after addition of 10 µM Mtb PanD WT in D 2 O at 298 K on a Bruker Avance 400 MHz spectrometer. Shown are ( c ) representative 1 H NMR spectra and ( d ) a plot of time-dependent β-Alanine formation at different incubation times by measuring the peak volume of converted L-Asp to β-Ala. At t = 40 min, ~50% conversion of L-aspartate to β-Alanine was observed as determined by integration of peak values. Thus, 40 min was chosen as a reference point within the linear range of PanD enzyme kinetics for subsequent enzyme assays. e Effect of POA on the formation of β-Ala by recombinant PanD WT and POA-resistant PanD 127TRASC131 proteins, respectively, as determined by 1 H NMR. The plot shows the results of a representative experiment. NMR spectra for e are shown in Supplementary Fig. 1 . Both recombinant proteins were purified as described 4 . The NMR experiments were repeated twice independently, yielding the same results. The results from a representative experiment are shown. Error bars were defined as 5% standard deviations. Source data are provided as a Source Data file. The cleaved form of the wild-type protein P2 migrates as a doublet with similar staining intensity. The reason for this behavior remains to be determined. LC–MS analysis of the doublet band suggests that both sub-bands present P2 (Supplementary Data 1 _P123seq). The P2 doublet is specific to recombinant wild-type protein and is not observed in the mutant PanD 127TRASC131 or in whole cell extracts (see Fig. 4 , western blot analyses). The SDS-PAGE analyses show that the recombinant PanD protein preparations used for in vitro analyses in the current study presented largely the cleaved, active form of the enzyme.

    Article Snippet: NMR experiments were carried out using a Bruker Avance 400 MHz NMR spectrometer, equipped on a 5 mm BBI probe head at 298 K as described by Sharma et al. .

    Techniques: Purification, Recombinant, Activity Assay, SDS Page, Binding Assay, Liquid Chromatography with Mass Spectroscopy, Synthesized, Nuclear Magnetic Resonance, Incubation, Staining, Mutagenesis, Western Blot, In Vitro

    (i) Integrated normalized polymer signals in the range of δ = 1–3 ppm as acquired in temperature-dependent 1 H-NMR spectra (circles; left and bottom axis, integrals are normalized on the lowest temperature) and (ii) extracted VPTTs (squares; right and top axis) for neat microgels containing different crosslinker content. Color code as indicated in the legend. Dashed line is guide to the eye. Solid lines are fits according to Equation (4).

    Journal: Gels

    Article Title: Interplay of the Influence of Crosslinker Content and Model Drugs on the Phase Transition of Thermoresponsive PNiPAM-BIS Microgels

    doi: 10.3390/gels8090571

    Figure Lengend Snippet: (i) Integrated normalized polymer signals in the range of δ = 1–3 ppm as acquired in temperature-dependent 1 H-NMR spectra (circles; left and bottom axis, integrals are normalized on the lowest temperature) and (ii) extracted VPTTs (squares; right and top axis) for neat microgels containing different crosslinker content. Color code as indicated in the legend. Dashed line is guide to the eye. Solid lines are fits according to Equation (4).

    Article Snippet: Temperature-dependent 1H spectra were taken on a Avance NEO 400 MHz NMR spectrometer (Bruker, Rheinstetten, Germany) equipped with a BB probe head (Bruker, Rheinstetten, Germany).

    Techniques: Nuclear Magnetic Resonance

    VPTT shift Δ T for different methods as a function of crosslinker content, as induced by the presence of ( a ) 20 mM m -HBA and ( b ) 2,4-DHBA as additives. Microgel concentrations are 1 wt.% (1 × 10 − 3 wt.% for DLS). Error bars reflect the standard deviation. The color code corresponds to different methods (DSC = red; DLS = blue; NMR = black).

    Journal: Gels

    Article Title: Interplay of the Influence of Crosslinker Content and Model Drugs on the Phase Transition of Thermoresponsive PNiPAM-BIS Microgels

    doi: 10.3390/gels8090571

    Figure Lengend Snippet: VPTT shift Δ T for different methods as a function of crosslinker content, as induced by the presence of ( a ) 20 mM m -HBA and ( b ) 2,4-DHBA as additives. Microgel concentrations are 1 wt.% (1 × 10 − 3 wt.% for DLS). Error bars reflect the standard deviation. The color code corresponds to different methods (DSC = red; DLS = blue; NMR = black).

    Article Snippet: Temperature-dependent 1H spectra were taken on a Avance NEO 400 MHz NMR spectrometer (Bruker, Rheinstetten, Germany) equipped with a BB probe head (Bruker, Rheinstetten, Germany).

    Techniques: Standard Deviation, Nuclear Magnetic Resonance

    Maximum of incorporated species P inc,max as a function of the transition temperature VPTT NMR for 2,4-DHBA (circles) and m -HBA (squares) for different crosslinker contents (blue x = 1, black x = 5, red x = 10, green x = 15). Dashed lines are guide to the eye and connect polymers of the same crosslinker content.

    Journal: Gels

    Article Title: Interplay of the Influence of Crosslinker Content and Model Drugs on the Phase Transition of Thermoresponsive PNiPAM-BIS Microgels

    doi: 10.3390/gels8090571

    Figure Lengend Snippet: Maximum of incorporated species P inc,max as a function of the transition temperature VPTT NMR for 2,4-DHBA (circles) and m -HBA (squares) for different crosslinker contents (blue x = 1, black x = 5, red x = 10, green x = 15). Dashed lines are guide to the eye and connect polymers of the same crosslinker content.

    Article Snippet: Temperature-dependent 1H spectra were taken on a Avance NEO 400 MHz NMR spectrometer (Bruker, Rheinstetten, Germany) equipped with a BB probe head (Bruker, Rheinstetten, Germany).

    Techniques: Nuclear Magnetic Resonance

    Partial atom connectivity map of 4c derived from 2D NMR data.

    Journal: The Journal of Organic Chemistry

    Article Title: Imidazolidine Hydride Donors in Palladium-Catalyzed Alkyne Hydroarylation

    doi: 10.1021/acs.joc.2c00725

    Figure Lengend Snippet: Partial atom connectivity map of 4c derived from 2D NMR data.

    Article Snippet: Support from the National Science Foundation (NSF) MRI program is acknowledged for the purchase of a Bruker D8 Venture Duo X-ray diffractometer (NSF-CHE-182117) and a Bruker Avance Neo 400 NMR spectrometer (NSF-CHE-2017828).

    Techniques: Derivative Assay, Nuclear Magnetic Resonance