global non-linear fitting program dynafit Search Results


dynafit software  (BioKin Ltd)
90
BioKin Ltd dynafit software
Dynafit Software, 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
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dynafit software - by Bioz Stars, 2026-05
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dynafit 3  (BioKin Ltd)
90
BioKin Ltd dynafit 3
Dynafit 3, 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
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dynafit 3 - by Bioz Stars, 2026-05
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dynafit  (BioKin Ltd)
90
BioKin Ltd dynafit
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
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dynafit - by Bioz Stars, 2026-05
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global non-linear fitting program dynafit  (BioKin Ltd)
90
BioKin Ltd global non-linear fitting program dynafit
(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.
Global Non Linear 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
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global non-linear fitting program dynafit - by Bioz Stars, 2026-05
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kintec explorer  (KinTek Corporation)
90
KinTek Corporation kintec explorer
(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.
Kintec Explorer, supplied by KinTek 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/kintec explorer/product/KinTek Corporation
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kintec explorer - by Bioz Stars, 2026-05
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scientist 3.0  (MicroMath Inc)
90
MicroMath Inc scientist 3.0
(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.
Scientist 3.0, supplied by MicroMath Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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scientist 3.0 - by Bioz Stars, 2026-05
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origin 2018  (OriginLab corp)
90
OriginLab corp origin 2018
(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.
Origin 2018, supplied by OriginLab corp, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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origin 2018 - by Bioz Stars, 2026-05
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origin software  (BioKin Ltd)
90
BioKin Ltd origin software
(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.
Origin Software, 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
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origin software - by Bioz Stars, 2026-05
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grafit 5.0.6  (ERITHACUS SOFTWARE LIMITED)
90
ERITHACUS SOFTWARE LIMITED grafit 5.0.6
(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.
Grafit 5.0.6, supplied by ERITHACUS SOFTWARE LIMITED, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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grafit 5.0.6 - by Bioz Stars, 2026-05
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graphpad prism software  (GraphPad Software Inc)
90
GraphPad Software Inc graphpad prism software
(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.
Graphpad Prism Software, supplied by GraphPad Software Inc, 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/graphpad prism software/product/GraphPad Software Inc
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graphpad prism software - by Bioz Stars, 2026-05
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program dynafit  (BioKin Ltd)
90
BioKin Ltd program dynafit
(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.
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/result/program dynafit/product/BioKin Ltd
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program dynafit - by Bioz Stars, 2026-05
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biokin dynafit  (BioKin Ltd)
90
BioKin Ltd biokin dynafit
(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.
Biokin 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
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Image Search Results


(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