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global fitting program dynafit  (BioKin Ltd)

 
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    BioKin Ltd global fitting program dynafit
    Global Fitting Program Dynafit, supplied by BioKin Ltd, 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/dynafit+fitting+program/global+fitting+program+dynafit/pm15269774-270-11-14
    Average 90 stars, based on 1 article reviews
    global fitting program dynafit - by Bioz Stars, 2026-10
    90/100 stars

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    other:

    Article Title: Periodic cycles of RNA unwinding and pausing by hepatitis C virus NS3 helicase.
    Article Snippet: 1.0.. Similarly, for chromatin immunoprecipitation, the ratio of selected and total DNA was calculated for each feature.. In this case the ratio found in euchromatin was arbitrarily set to 1.0 in both mutant and wild type, as recovery of immunoselected DNA is always much less than 100%.

    Article Title: Uncaging carbon disulfide. Delivery platforms for potential pharmacological applications: a mechanistic approach
    Article Snippet: Kinetics data were processed using IgorPro 6.37 software by Wavemetrics, Inc., and Prism 7 by GraphPad Software, Inc. For global fittings of equilibrium analyses and determination of back reaction values, a DynaFit (BioKin Ltd) nonlinear least squares regression program was used.

    Article Title: Colorimetric determination of Cu2+ in simulated wastewater using naphthalimide-based Schiff base
    Article Snippet: Accepted Manuscript Colorimetric determination of Cu2+ in simulated wastewater using naphthali- mide-based Schiff base In Jung Chang, Myung Gil Choi, Yong Ae Jeong, Sang Hun Lee, Suk-Kyu Chang PII: S0040-4039(16)31721-X DOI: http://dx.doi.org/10.1016/j.tetlet.2016.12.066 Reference: TETL 48478 To appear in: Tetrahedron Letters Received Date: 26 October 2016 Revised Date: 20 December 2016 Accepted Date: 22 December 2016 Please cite this article as: Jung Chang, I., Gil Choi, M., Ae Jeong, Y., Hun Lee, S., Chang, S-K., Colorimetric determination of Cu2+ in simulated wastewater using naphthalimide-based Schiff base, Tetrahedron Letters (2016), doi: http://dx.doi.org/10.1016/j.tetlet.2016.12.066 This is a PDF file of an unedited manuscript that has been accepted for publication.. As a service to our customers we are providing this early version of the manuscript.. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form.

    Article Title: Active-site directed chemical tools for profiling mitochondrial Lon protease
    Article Snippet: The solid lines represent the best fit of the data, as described in Materials and Methods. ( c ) Experimental time courses were fit to both one-step and two-step inhibition mechanisms using the global non-linear fitting program, DynaFit (Biokin, Ltd.).

    Article Title: Real-time monitoring of a stepwise transcription reaction on a quartz-crystal microbalance.
    Article Snippet: 0003-2697/$ see front matter 2011 Elsevier Inc. A doi:10.1016/j.ab.2011.11.019 ⇑ Corresponding author.. Fax: +81 45 924 5836.. E-mail address: yokahata@bio.titech.ac.jp (Y. Okah 1 Abbreviations used: CC, closed complex; EC, elo complex; PBD, promoter-binding domain; PCR, polym quartz-crystal microbalance; RNAP, RNA polymerase; wild type.

    Software:

    Article Title: Biological Thiols and Carbon Disulfide: The Formation and Decay of Trithiocarbonates under Physiologically Relevant Conditions
    Article Snippet: .. Kinetics data were processed using Igor Pro 6.37 software by WaveMetrics, Inc., and Prism 7 by GraphPad Software, Inc. For global fittings of equilibrium analyses and determination of back-reaction values, a DynaFit (BioKin Ltd) nonlinear least-squares regression program was used. ..

    Inhibition:

    Article Title: Active-site directed chemical tools for profiling mitochondrial Lon protease
    Article Snippet: .. To support the two-step mechanism, the experimental time courses were globally fitted to both a one- and a two-step inhibition mechanism using the nonlinear fitting program Dynafit (Biokin) ( 26 ) ( , panel c ). ..



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    (a) Representative time course of peptide cleavage by human Lon in the presence of ATP and DBN93. Two rates of cleavage, vi and vss, and a rate constant of interconversion between the two, kinter, can be quantified from the experimental time course. (b) Reactions containing 150 nM human Lon were preincubated with 1 mM FRETN 89–98 prior to the addition of 1 mM ATP. After 90 s, varying amounts of DBN93 (0–2 µM) were added and peptide hydrolysis was monitored over 45 min. All experiments were done in at least duplicate and the vi and vss values determined by fitting the time courses as done previously for bacterial Lon (23). The averaged vi (■), vss (▲) in the presence of inhibitor normalized to 1 with the average velocity in the absence of inhibitor were plotted against corresponding inhibitor concentrations. The solid lines represent the best fit of the data, as described in Materials and Methods. (c) Experimental time courses were fit to both one-step and two-step inhibition mechanisms using the global non-linear fitting program, <t>DynaFit</t> (Biokin, Ltd.). Black lines represent the averaged experimental time courses at 150 nM hLon, 1 mM ATP, 1 mM peptide and varying concentrations of DBN93. Gray lines represent the best fit of the data to the two-step time-dependent mechanism which was most consistent with the experimental data. The kinetic parameters yielded from this fit are summarized and compared to those previously determined for bacterial Lon (23) in Table 1.
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    (a) Representative time course of peptide cleavage by human Lon in the presence of ATP and DBN93. Two rates of cleavage, vi and vss, and a rate constant of interconversion between the two, kinter, can be quantified from the experimental time course. (b) Reactions containing 150 nM human Lon were preincubated with 1 mM FRETN 89–98 prior to the addition of 1 mM ATP. After 90 s, varying amounts of DBN93 (0–2 µM) were added and peptide hydrolysis was monitored over 45 min. All experiments were done in at least duplicate and the vi and vss values determined by fitting the time courses as done previously for bacterial Lon (23). The averaged vi (■), vss (▲) in the presence of inhibitor normalized to 1 with the average velocity in the absence of inhibitor were plotted against corresponding inhibitor concentrations. The solid lines represent the best fit of the data, as described in Materials and Methods. (c) Experimental time courses were fit to both one-step and two-step inhibition mechanisms using the global non-linear fitting program, <t>DynaFit</t> (Biokin, Ltd.). Black lines represent the averaged experimental time courses at 150 nM hLon, 1 mM ATP, 1 mM peptide and varying concentrations of DBN93. Gray lines represent the best fit of the data to the two-step time-dependent mechanism which was most consistent with the experimental data. The kinetic parameters yielded from this fit are summarized and compared to those previously determined for bacterial Lon (23) in Table 1.
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    global fitting program dynafit  (BioKin Ltd)
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    (a) Representative time course of peptide cleavage by human Lon in the presence of ATP and DBN93. Two rates of cleavage, vi and vss, and a rate constant of interconversion between the two, kinter, can be quantified from the experimental time course. (b) Reactions containing 150 nM human Lon were preincubated with 1 mM FRETN 89–98 prior to the addition of 1 mM ATP. After 90 s, varying amounts of DBN93 (0–2 µM) were added and peptide hydrolysis was monitored over 45 min. All experiments were done in at least duplicate and the vi and vss values determined by fitting the time courses as done previously for bacterial Lon (23). The averaged vi (■), vss (▲) in the presence of inhibitor normalized to 1 with the average velocity in the absence of inhibitor were plotted against corresponding inhibitor concentrations. The solid lines represent the best fit of the data, as described in Materials and Methods. (c) Experimental time courses were fit to both one-step and two-step inhibition mechanisms using the global non-linear fitting program, <t>DynaFit</t> (Biokin, Ltd.). Black lines represent the averaged experimental time courses at 150 nM hLon, 1 mM ATP, 1 mM peptide and varying concentrations of DBN93. Gray lines represent the best fit of the data to the two-step time-dependent mechanism which was most consistent with the experimental data. The kinetic parameters yielded from this fit are summarized and compared to those previously determined for bacterial Lon (23) in Table 1.
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    (a) Representative time course of peptide cleavage by human Lon in the presence of ATP and DBN93. Two rates of cleavage, vi and vss, and a rate constant of interconversion between the two, kinter, can be quantified from the experimental time course. (b) Reactions containing 150 nM human Lon were preincubated with 1 mM FRETN 89–98 prior to the addition of 1 mM ATP. After 90 s, varying amounts of DBN93 (0–2 µM) were added and peptide hydrolysis was monitored over 45 min. All experiments were done in at least duplicate and the vi and vss values determined by fitting the time courses as done previously for bacterial Lon (23). The averaged vi (■), vss (▲) in the presence of inhibitor normalized to 1 with the average velocity in the absence of inhibitor were plotted against corresponding inhibitor concentrations. The solid lines represent the best fit of the data, as described in Materials and Methods. (c) Experimental time courses were fit to both one-step and two-step inhibition mechanisms using the global non-linear fitting program, DynaFit (Biokin, Ltd.). Black lines represent the averaged experimental time courses at 150 nM hLon, 1 mM ATP, 1 mM peptide and varying concentrations of DBN93. Gray lines represent the best fit of the data to the two-step time-dependent mechanism which was most consistent with the experimental data. The kinetic parameters yielded from this fit are summarized and compared to those previously determined for bacterial Lon (23) in Table 1.

    Journal: ACS chemical biology

    Article Title: Active-site directed chemical tools for profiling mitochondrial Lon protease

    doi: 10.1021/cb100408w

    Figure Lengend Snippet: (a) Representative time course of peptide cleavage by human Lon in the presence of ATP and DBN93. Two rates of cleavage, vi and vss, and a rate constant of interconversion between the two, kinter, can be quantified from the experimental time course. (b) Reactions containing 150 nM human Lon were preincubated with 1 mM FRETN 89–98 prior to the addition of 1 mM ATP. After 90 s, varying amounts of DBN93 (0–2 µM) were added and peptide hydrolysis was monitored over 45 min. All experiments were done in at least duplicate and the vi and vss values determined by fitting the time courses as done previously for bacterial Lon (23). The averaged vi (■), vss (▲) in the presence of inhibitor normalized to 1 with the average velocity in the absence of inhibitor were plotted against corresponding inhibitor concentrations. The solid lines represent the best fit of the data, as described in Materials and Methods. (c) Experimental time courses were fit to both one-step and two-step inhibition mechanisms using the global non-linear fitting program, DynaFit (Biokin, Ltd.). Black lines represent the averaged experimental time courses at 150 nM hLon, 1 mM ATP, 1 mM peptide and varying concentrations of DBN93. Gray lines represent the best fit of the data to the two-step time-dependent mechanism which was most consistent with the experimental data. The kinetic parameters yielded from this fit are summarized and compared to those previously determined for bacterial Lon (23) in Table 1.

    Article Snippet: The solid lines represent the best fit of the data, as described in Materials and Methods. ( c ) Experimental time courses were fit to both one-step and two-step inhibition mechanisms using the global non-linear fitting program, DynaFit (Biokin, Ltd.).

    Techniques: Inhibition

    Kinetic parameters of inhibition of human Lon peptidase activity by DBN93 as determined by global fitting of experimental data using DynaFit. The resultant values are compared to those previously determined for bacterial Lon. Reported errors are s.e.m.

    Journal: ACS chemical biology

    Article Title: Active-site directed chemical tools for profiling mitochondrial Lon protease

    doi: 10.1021/cb100408w

    Figure Lengend Snippet: Kinetic parameters of inhibition of human Lon peptidase activity by DBN93 as determined by global fitting of experimental data using DynaFit. The resultant values are compared to those previously determined for bacterial Lon. Reported errors are s.e.m.

    Article Snippet: The solid lines represent the best fit of the data, as described in Materials and Methods. ( c ) Experimental time courses were fit to both one-step and two-step inhibition mechanisms using the global non-linear fitting program, DynaFit (Biokin, Ltd.).

    Techniques: Inhibition, Activity Assay

    (a) Representative time course of peptide cleavage by human Lon in the presence of ATP and DBN93. Two rates of cleavage, vi and vss, and a rate constant of interconversion between the two, kinter, can be quantified from the experimental time course. (b) Reactions containing 150 nM human Lon were preincubated with 1 mM FRETN 89–98 prior to the addition of 1 mM ATP. After 90 s, varying amounts of DBN93 (0–2 µM) were added and peptide hydrolysis was monitored over 45 min. All experiments were done in at least duplicate and the vi and vss values determined by fitting the time courses as done previously for bacterial Lon (23). The averaged vi (■), vss (▲) in the presence of inhibitor normalized to 1 with the average velocity in the absence of inhibitor were plotted against corresponding inhibitor concentrations. The solid lines represent the best fit of the data, as described in Materials and Methods. (c) Experimental time courses were fit to both one-step and two-step inhibition mechanisms using the global non-linear fitting program, DynaFit (Biokin, Ltd.). Black lines represent the averaged experimental time courses at 150 nM hLon, 1 mM ATP, 1 mM peptide and varying concentrations of DBN93. Gray lines represent the best fit of the data to the two-step time-dependent mechanism which was most consistent with the experimental data. The kinetic parameters yielded from this fit are summarized and compared to those previously determined for bacterial Lon (23) in Table 1.

    Journal: ACS chemical biology

    Article Title: Active-site directed chemical tools for profiling mitochondrial Lon protease

    doi: 10.1021/cb100408w

    Figure Lengend Snippet: (a) Representative time course of peptide cleavage by human Lon in the presence of ATP and DBN93. Two rates of cleavage, vi and vss, and a rate constant of interconversion between the two, kinter, can be quantified from the experimental time course. (b) Reactions containing 150 nM human Lon were preincubated with 1 mM FRETN 89–98 prior to the addition of 1 mM ATP. After 90 s, varying amounts of DBN93 (0–2 µM) were added and peptide hydrolysis was monitored over 45 min. All experiments were done in at least duplicate and the vi and vss values determined by fitting the time courses as done previously for bacterial Lon (23). The averaged vi (■), vss (▲) in the presence of inhibitor normalized to 1 with the average velocity in the absence of inhibitor were plotted against corresponding inhibitor concentrations. The solid lines represent the best fit of the data, as described in Materials and Methods. (c) Experimental time courses were fit to both one-step and two-step inhibition mechanisms using the global non-linear fitting program, DynaFit (Biokin, Ltd.). Black lines represent the averaged experimental time courses at 150 nM hLon, 1 mM ATP, 1 mM peptide and varying concentrations of DBN93. Gray lines represent the best fit of the data to the two-step time-dependent mechanism which was most consistent with the experimental data. The kinetic parameters yielded from this fit are summarized and compared to those previously determined for bacterial Lon (23) in Table 1.

    Article Snippet: To support the two-step mechanism, the experimental time courses were globally fitted to both a one- and a two-step inhibition mechanism using the nonlinear fitting program Dynafit (Biokin) ( 26 ) ( , panel c ).

    Techniques: Inhibition

    Kinetic parameters of inhibition of human Lon peptidase activity by DBN93 as determined by global fitting of experimental data using DynaFit. The resultant values are compared to those previously determined for bacterial Lon. Reported errors are s.e.m.

    Journal: ACS chemical biology

    Article Title: Active-site directed chemical tools for profiling mitochondrial Lon protease

    doi: 10.1021/cb100408w

    Figure Lengend Snippet: Kinetic parameters of inhibition of human Lon peptidase activity by DBN93 as determined by global fitting of experimental data using DynaFit. The resultant values are compared to those previously determined for bacterial Lon. Reported errors are s.e.m.

    Article Snippet: To support the two-step mechanism, the experimental time courses were globally fitted to both a one- and a two-step inhibition mechanism using the nonlinear fitting program Dynafit (Biokin) ( 26 ) ( , panel c ).

    Techniques: Inhibition, Activity Assay