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program dynafit  (BioKin Ltd)

 
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    BioKin Ltd program dynafit
    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/global+non-linear+fitting+program+dynafit/dynafit+program/pmc02645938-151-12-14
    Average 90 stars, based on 1 article reviews
    program dynafit - by Bioz Stars, 2026-11
    90/100 stars

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    Related Articles

    UV-Vis Spectroscopy:

    Article Title: Sequence-selective encapsulation and protection of long peptides by a self-assembled Fe II 8 L 6 cubic cage
    Article Snippet: .. Host-guest model: The experimental data obtained using UV-Vis spectroscopy for each guest was fitted using nonlinear analysis with DynaFit program (Biokin Software)2 to the binding equation derived for 1:1 model porphyrin:imidazole group (non-cooperative model). ..

    Software:

    Article Title: Sequence-selective encapsulation and protection of long peptides by a self-assembled Fe II 8 L 6 cubic cage
    Article Snippet: .. Host-guest model: The experimental data obtained using UV-Vis spectroscopy for each guest was fitted using nonlinear analysis with DynaFit program (Biokin Software)2 to the binding equation derived for 1:1 model porphyrin:imidazole group (non-cooperative model). ..

    Article Title: Supramolecular Catalysis of Acyl Transfer within Zinc Porphyrin-Based Metal-Organic Cages.
    Article Snippet: To illustrate the supramolecular catalysis process in molecular containers, two porphyrinatozinc(II)-faced cubic cages with different sizes were synthesized and used to catalyze acyltransfer reactions between N-acetylimidazole (NAI) and various pyridylcarbinol (PC) regioisomers (2-PC, 3-PC, and 4-PC).. A systemic investigation of the supramolecular catalysis occurring within these two hosts was performed, in combination with a host− guest binding study and density functional theory calculations.. Compared to the reaction in a bulk solvent, the results that the reaction of 2-PC was found to be highly efficient with high rate enhancements (kcat/kuncat = 283 for Zn-1 and 442 for Zn-2), as well as the different efficiencies of the reactions with various ortho-substituted 2-PC substrates and NAI derivates should be attributed to the cages having preconcentrated and preoriented substrates.

    Binding Assay:

    Article Title: Sequence-selective encapsulation and protection of long peptides by a self-assembled Fe II 8 L 6 cubic cage
    Article Snippet: .. Host-guest model: The experimental data obtained using UV-Vis spectroscopy for each guest was fitted using nonlinear analysis with DynaFit program (Biokin Software)2 to the binding equation derived for 1:1 model porphyrin:imidazole group (non-cooperative model). ..

    Article Title: Sequence-selective encapsulation and protection of long peptides by a self-assembled Fe II 8 L 6 cubic cage
    Article Snippet: .. Data obtained from the ultraviolet–visible titration were then fitted using nonlinear analysis with DynaFit programme (Biokin Software) to the binding equation derived for either 1:1 model (porphyrin:guest with one imidazole group) or 2:1 model (porphyrin:guest with two imidazole groups), except in the case of G7 . ..

    Article Title: Supramolecular Catalysis of Acyl Transfer within Zinc Porphyrin-Based Metal-Organic Cages.
    Article Snippet: To illustrate the supramolecular catalysis process in molecular containers, two porphyrinatozinc(II)-faced cubic cages with different sizes were synthesized and used to catalyze acyltransfer reactions between N-acetylimidazole (NAI) and various pyridylcarbinol (PC) regioisomers (2-PC, 3-PC, and 4-PC).. A systemic investigation of the supramolecular catalysis occurring within these two hosts was performed, in combination with a host− guest binding study and density functional theory calculations.. Compared to the reaction in a bulk solvent, the results that the reaction of 2-PC was found to be highly efficient with high rate enhancements (kcat/kuncat = 283 for Zn-1 and 442 for Zn-2), as well as the different efficiencies of the reactions with various ortho-substituted 2-PC substrates and NAI derivates should be attributed to the cages having preconcentrated and preoriented substrates.

    Derivative Assay:

    Article Title: Sequence-selective encapsulation and protection of long peptides by a self-assembled Fe II 8 L 6 cubic cage
    Article Snippet: .. Host-guest model: The experimental data obtained using UV-Vis spectroscopy for each guest was fitted using nonlinear analysis with DynaFit program (Biokin Software)2 to the binding equation derived for 1:1 model porphyrin:imidazole group (non-cooperative model). ..

    Article Title: Sequence-selective encapsulation and protection of long peptides by a self-assembled Fe II 8 L 6 cubic cage
    Article Snippet: .. Data obtained from the ultraviolet–visible titration were then fitted using nonlinear analysis with DynaFit programme (Biokin Software) to the binding equation derived for either 1:1 model (porphyrin:guest with one imidazole group) or 2:1 model (porphyrin:guest with two imidazole groups), except in the case of G7 . ..

    Article Title: Supramolecular Catalysis of Acyl Transfer within Zinc Porphyrin-Based Metal-Organic Cages.
    Article Snippet: To illustrate the supramolecular catalysis process in molecular containers, two porphyrinatozinc(II)-faced cubic cages with different sizes were synthesized and used to catalyze acyltransfer reactions between N-acetylimidazole (NAI) and various pyridylcarbinol (PC) regioisomers (2-PC, 3-PC, and 4-PC).. A systemic investigation of the supramolecular catalysis occurring within these two hosts was performed, in combination with a host− guest binding study and density functional theory calculations.. Compared to the reaction in a bulk solvent, the results that the reaction of 2-PC was found to be highly efficient with high rate enhancements (kcat/kuncat = 283 for Zn-1 and 442 for Zn-2), as well as the different efficiencies of the reactions with various ortho-substituted 2-PC substrates and NAI derivates should be attributed to the cages having preconcentrated and preoriented substrates.

    Control:

    Article Title: Chikungunya nsP2 protease is not a papain-like cysteine protease and the catalytic dyad cysteine is interchangeable with a proximal serine.
    Article Snippet: Protease activity was followed by continuously monitoring for 3 hr increasing fluorescence (substrate depletion) using a Beckman Coulter DTX880 multimode detector at 340 nm excitation and 430 nm emission wavelengths at 37 °C. .. To obtain the kinetic parameters, control curves with no enzyme were subtracted from the enzyme progress curves, which were then analyzed by Dynafit program© version 3.28.070 (BioKin, Ltd.)48. ..

    Titration:

    Article Title: Sequence-selective encapsulation and protection of long peptides by a self-assembled Fe II 8 L 6 cubic cage
    Article Snippet: .. Data obtained from the ultraviolet–visible titration were then fitted using nonlinear analysis with DynaFit programme (Biokin Software) to the binding equation derived for either 1:1 model (porphyrin:guest with one imidazole group) or 2:1 model (porphyrin:guest with two imidazole groups), except in the case of G7 . ..

    Article Title: Supramolecular Catalysis of Acyl Transfer within Zinc Porphyrin-Based Metal-Organic Cages.
    Article Snippet: To illustrate the supramolecular catalysis process in molecular containers, two porphyrinatozinc(II)-faced cubic cages with different sizes were synthesized and used to catalyze acyltransfer reactions between N-acetylimidazole (NAI) and various pyridylcarbinol (PC) regioisomers (2-PC, 3-PC, and 4-PC).. A systemic investigation of the supramolecular catalysis occurring within these two hosts was performed, in combination with a host− guest binding study and density functional theory calculations.. Compared to the reaction in a bulk solvent, the results that the reaction of 2-PC was found to be highly efficient with high rate enhancements (kcat/kuncat = 283 for Zn-1 and 442 for Zn-2), as well as the different efficiencies of the reactions with various ortho-substituted 2-PC substrates and NAI derivates should be attributed to the cages having preconcentrated and preoriented substrates.

    Comparison:

    Article Title: Discovery of novel drug-like antitubercular hits targeting the MEP pathway enzyme DXPS by strategic application of ligand-based virtual screening
    Article Snippet: .. Initial rate values were evaluated with a nonlinear regression method using the program Dynafit (Biokin, http://www.biokin.com/dynafit/).13 MOI information was achieved by comparison of IC50 values under different conditions in duplicates. ..

    Fluorescence:

    Article Title: Small-molecule allosteric inhibitors of BAX
    Article Snippet: .. We used the program DYNAFIT (BioKin) to simulate the competition of BAI1 with vMIA and tested this using a fluorescence polarization assay with the vMIA peptide and BAX. ..

    Concentration Assay:

    Article Title: Flatbed-scanner-based colorimetric Cu2+ signaling system derived from a coumarin–benzopyrylium conjugated dye
    Article Snippet: In this study, we developed a flatbed-scanner-based Cu-selective signaling method using a coumarin–benzopyrylium conjugated dye platform.. The designed sensors (CB-1 and CB-2) were readily synthesized by the reaction of coumarin–benzopyrylium hydrazide with salicylaldehyde or 2-hydroxynaphthaldehyde, respectively.. Sensor CB-1 exhibited pronounced colorimetric and fluorescence signaling behaviors toward Cu ions in 50% aqueous acetate buffered (pH 4.7) acetonitrile solution.

    other:

    Article Title: Interaction features of adenine DNA glycosylase MutY from E. coli with DNA substrates
    Article Snippet: Kinetic characteristics of specific recognition of damaged base by the DNA glycosylase MutY in model DNA substrates, containing oxoG/A-, G/A-, oxoG/Cand F/G pairs in the central position, were investigated.. Conformational changes of the MutY enzyme during the recognition of the damaged base in DNA have been recorded by the change in the f luorescence intensity of tryptophan residues using the stopped-flow technique in real time.. DNA duplexes containing a f luorescein residue were used for the registration of DNA conformational changes.



    Similar Products

    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
    https://www.bioz.com/product/global+non-linear+fitting+program+dynafit/global+fitting+program+dynafit/pmc03158820-67-37-38
    Average 90 stars, based on 1 article reviews
    global non-linear fitting program dynafit - by Bioz Stars, 2026-11
    90/100 stars
    		  Buy from Supplier

    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