dsf data Search Results


dsf data  (GraphPad Software Inc)
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GraphPad Software Inc dsf data
Dsf Data, 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/dsf data/product/GraphPad Software Inc
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dsf data - by Bioz Stars, 2026-03
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dsf data for biolog assays  (Biolog Inc)
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Biolog Inc dsf data for biolog assays
( a ) Thermal denaturation of SAR11_1179 in the absence (black) or presence (red) of 1 mM Na 2 HPO 4 measured by DSF (Δ T M = 10.9 ± 0.4 °C, mean ± s.d., n = 3 technical replicates). ( b - c ) Representative <t>ITC</t> data for titration of 23 µM SAR11_1179 with 185 µM Na 2 HPO 4 in the absence ( b ) or presence ( c ) of 28 mM Na 2 SO 4 . Fitting the data to the one-set-of-sites model gave a K d of 133 ± 28 nM in the absence of sulfate and 892 ± 122 nM in the presence of 28 mM sulfate (mean ± s.d., n = 3 or 4 replicate titrations; significantly different by two-tailed t -test on log 10 K d values; P = 3.03 × 10 −5 , t = 14.28, df = 5, difference between means = 0.831, 95% confidence interval = 0.681 to 0.981). ( d ) UV-visible spectrum of SAR11_1238 purified from E. coli , without addition of ligand, showing presence of endogenously bound iron(III). ( e - f ) UV-visible spectra of unliganded SAR11_1238 titrated with iron(III) delivered as ( e ) iron(III) citrate or ( f ) ammonium iron(II) sulfate (see section for further explanation). ( g - h ) Titration of SAR11_1238 with iron(III) delivered as ( g ) iron(III) citrate or ( h ) ammonium iron(II) sulfate, monitored by absorbance at 440 nm. Discrete data points from four (g) or two (h) technical replicates (independent titrations) are shown. The line represents a fit to the linear portion of the titration. ( i ) Competitive titration of iron(III)-bound SAR11_1238 with citrate, monitored by absorbance at 440 nm. Results from two technical replicates (independent titrations) are shown as discrete data points.
Dsf Data For Biolog Assays, supplied by Biolog 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/dsf data for biolog assays/product/Biolog Inc
Average 90 stars, based on 1 article reviews
dsf data for biolog assays - by Bioz Stars, 2026-03
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temperature data-fire in dsf with venetian blinds  (Mendeley Ltd)
90
Mendeley Ltd temperature data-fire in dsf with venetian blinds
( a ) Thermal denaturation of SAR11_1179 in the absence (black) or presence (red) of 1 mM Na 2 HPO 4 measured by DSF (Δ T M = 10.9 ± 0.4 °C, mean ± s.d., n = 3 technical replicates). ( b - c ) Representative <t>ITC</t> data for titration of 23 µM SAR11_1179 with 185 µM Na 2 HPO 4 in the absence ( b ) or presence ( c ) of 28 mM Na 2 SO 4 . Fitting the data to the one-set-of-sites model gave a K d of 133 ± 28 nM in the absence of sulfate and 892 ± 122 nM in the presence of 28 mM sulfate (mean ± s.d., n = 3 or 4 replicate titrations; significantly different by two-tailed t -test on log 10 K d values; P = 3.03 × 10 −5 , t = 14.28, df = 5, difference between means = 0.831, 95% confidence interval = 0.681 to 0.981). ( d ) UV-visible spectrum of SAR11_1238 purified from E. coli , without addition of ligand, showing presence of endogenously bound iron(III). ( e - f ) UV-visible spectra of unliganded SAR11_1238 titrated with iron(III) delivered as ( e ) iron(III) citrate or ( f ) ammonium iron(II) sulfate (see section for further explanation). ( g - h ) Titration of SAR11_1238 with iron(III) delivered as ( g ) iron(III) citrate or ( h ) ammonium iron(II) sulfate, monitored by absorbance at 440 nm. Discrete data points from four (g) or two (h) technical replicates (independent titrations) are shown. The line represents a fit to the linear portion of the titration. ( i ) Competitive titration of iron(III)-bound SAR11_1238 with citrate, monitored by absorbance at 440 nm. Results from two technical replicates (independent titrations) are shown as discrete data points.
Temperature Data Fire In Dsf With Venetian Blinds, supplied by Mendeley 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/temperature data-fire in dsf with venetian blinds/product/Mendeley Ltd
Average 90 stars, based on 1 article reviews
temperature data-fire in dsf with venetian blinds - by Bioz Stars, 2026-03
90/100 stars
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Image Search Results


( a ) Thermal denaturation of SAR11_1179 in the absence (black) or presence (red) of 1 mM Na 2 HPO 4 measured by DSF (Δ T M = 10.9 ± 0.4 °C, mean ± s.d., n = 3 technical replicates). ( b - c ) Representative ITC data for titration of 23 µM SAR11_1179 with 185 µM Na 2 HPO 4 in the absence ( b ) or presence ( c ) of 28 mM Na 2 SO 4 . Fitting the data to the one-set-of-sites model gave a K d of 133 ± 28 nM in the absence of sulfate and 892 ± 122 nM in the presence of 28 mM sulfate (mean ± s.d., n = 3 or 4 replicate titrations; significantly different by two-tailed t -test on log 10 K d values; P = 3.03 × 10 −5 , t = 14.28, df = 5, difference between means = 0.831, 95% confidence interval = 0.681 to 0.981). ( d ) UV-visible spectrum of SAR11_1238 purified from E. coli , without addition of ligand, showing presence of endogenously bound iron(III). ( e - f ) UV-visible spectra of unliganded SAR11_1238 titrated with iron(III) delivered as ( e ) iron(III) citrate or ( f ) ammonium iron(II) sulfate (see section for further explanation). ( g - h ) Titration of SAR11_1238 with iron(III) delivered as ( g ) iron(III) citrate or ( h ) ammonium iron(II) sulfate, monitored by absorbance at 440 nm. Discrete data points from four (g) or two (h) technical replicates (independent titrations) are shown. The line represents a fit to the linear portion of the titration. ( i ) Competitive titration of iron(III)-bound SAR11_1238 with citrate, monitored by absorbance at 440 nm. Results from two technical replicates (independent titrations) are shown as discrete data points.

Journal: Nature

Article Title: The ultra-high affinity transport proteins of ubiquitous marine bacteria

doi: 10.1038/s41586-024-07924-w

Figure Lengend Snippet: ( a ) Thermal denaturation of SAR11_1179 in the absence (black) or presence (red) of 1 mM Na 2 HPO 4 measured by DSF (Δ T M = 10.9 ± 0.4 °C, mean ± s.d., n = 3 technical replicates). ( b - c ) Representative ITC data for titration of 23 µM SAR11_1179 with 185 µM Na 2 HPO 4 in the absence ( b ) or presence ( c ) of 28 mM Na 2 SO 4 . Fitting the data to the one-set-of-sites model gave a K d of 133 ± 28 nM in the absence of sulfate and 892 ± 122 nM in the presence of 28 mM sulfate (mean ± s.d., n = 3 or 4 replicate titrations; significantly different by two-tailed t -test on log 10 K d values; P = 3.03 × 10 −5 , t = 14.28, df = 5, difference between means = 0.831, 95% confidence interval = 0.681 to 0.981). ( d ) UV-visible spectrum of SAR11_1238 purified from E. coli , without addition of ligand, showing presence of endogenously bound iron(III). ( e - f ) UV-visible spectra of unliganded SAR11_1238 titrated with iron(III) delivered as ( e ) iron(III) citrate or ( f ) ammonium iron(II) sulfate (see section for further explanation). ( g - h ) Titration of SAR11_1238 with iron(III) delivered as ( g ) iron(III) citrate or ( h ) ammonium iron(II) sulfate, monitored by absorbance at 440 nm. Discrete data points from four (g) or two (h) technical replicates (independent titrations) are shown. The line represents a fit to the linear portion of the titration. ( i ) Competitive titration of iron(III)-bound SAR11_1238 with citrate, monitored by absorbance at 440 nm. Results from two technical replicates (independent titrations) are shown as discrete data points.

Article Snippet: Raw ITC data, DSF data for Biolog assays, GC–MS data, phylogenetic and biogeographical data, and source data for figures are available via the Open Science Framework (10.17605/OSF.IO/47TR5).

Techniques: Titration, Two Tailed Test, Purification

We measured the change in denaturation temperature (Δ T M ) in the presence of 10 mM ligand by DSF. Ligands that resulted in a significant increase in T M (≥2 °C) at a concentration of 10 mM are shown. Protein–ligand interactions that were verified by ITC are labelled with the measured K d value for the interaction. Columns represent the mean of two technical replicates shown as individual data points. Only proteins with a high-affinity ligand confirmed by ITC are shown. The DSF results show only significant protein–ligand interactions in vitro; whether these interactions are biologically important depends on the binding affinity and the environmental concentration of the ligand. Dagger indicates that the value is from the literature . DHPS, 2,3-dihydroxypropane-1-sulfonate; GABA, γ-aminobutyrate.

Journal: Nature

Article Title: The ultra-high affinity transport proteins of ubiquitous marine bacteria

doi: 10.1038/s41586-024-07924-w

Figure Lengend Snippet: We measured the change in denaturation temperature (Δ T M ) in the presence of 10 mM ligand by DSF. Ligands that resulted in a significant increase in T M (≥2 °C) at a concentration of 10 mM are shown. Protein–ligand interactions that were verified by ITC are labelled with the measured K d value for the interaction. Columns represent the mean of two technical replicates shown as individual data points. Only proteins with a high-affinity ligand confirmed by ITC are shown. The DSF results show only significant protein–ligand interactions in vitro; whether these interactions are biologically important depends on the binding affinity and the environmental concentration of the ligand. Dagger indicates that the value is from the literature . DHPS, 2,3-dihydroxypropane-1-sulfonate; GABA, γ-aminobutyrate.

Article Snippet: Raw ITC data, DSF data for Biolog assays, GC–MS data, phylogenetic and biogeographical data, and source data for figures are available via the Open Science Framework (10.17605/OSF.IO/47TR5).

Techniques: Concentration Assay, In Vitro, Binding Assay

a , Comparison of K d values for SBPs from Ca . P. ubique HTCC1062 with bacterial SBPs previously reported in the literature ( n = 206; Supplementary Data ). In cases where the SBP binds multiple ligands, data for the highest-affinity ligand is shown. SBPs with K d < 5 nM are highlighted by red shading. b , K d values for the highest-affinity interaction for each SBP from Ca . P. ubique HTCC1062. Values for SAR11_0655 and SAR11_0769 represent upper bounds on K d (lower bounds on affinity). Bars represent mean of 2–5 technical replicates (independent titrations), shown as individual data points. Data from the literature data are shown for SAR11_1302 . c , d , Determination of binding parameters for high-affinity interactions using competitive ITC experiments. Data fitting was performed in MicroCal PEAQ software. c , Simultaneous titration of SAR11_1210 and SeArgT with l -arginine. Data are representative of two replicates (separate titrations). d , Titration of SAR11_0769 with d -glucose, showing a biphasic binding curve. Data are representative of four replicates (separate titrations). The negative control titration (buffer plus d -glucose) is shown in grey. e , Binding mode of l -arginine in the crystal structure of SAR11_1210 (1.32 Å resolution). f , Binding mode of d -glucose in the crystal structure of SAR11_0769 (1.86 Å resolution).

Journal: Nature

Article Title: The ultra-high affinity transport proteins of ubiquitous marine bacteria

doi: 10.1038/s41586-024-07924-w

Figure Lengend Snippet: a , Comparison of K d values for SBPs from Ca . P. ubique HTCC1062 with bacterial SBPs previously reported in the literature ( n = 206; Supplementary Data ). In cases where the SBP binds multiple ligands, data for the highest-affinity ligand is shown. SBPs with K d < 5 nM are highlighted by red shading. b , K d values for the highest-affinity interaction for each SBP from Ca . P. ubique HTCC1062. Values for SAR11_0655 and SAR11_0769 represent upper bounds on K d (lower bounds on affinity). Bars represent mean of 2–5 technical replicates (independent titrations), shown as individual data points. Data from the literature data are shown for SAR11_1302 . c , d , Determination of binding parameters for high-affinity interactions using competitive ITC experiments. Data fitting was performed in MicroCal PEAQ software. c , Simultaneous titration of SAR11_1210 and SeArgT with l -arginine. Data are representative of two replicates (separate titrations). d , Titration of SAR11_0769 with d -glucose, showing a biphasic binding curve. Data are representative of four replicates (separate titrations). The negative control titration (buffer plus d -glucose) is shown in grey. e , Binding mode of l -arginine in the crystal structure of SAR11_1210 (1.32 Å resolution). f , Binding mode of d -glucose in the crystal structure of SAR11_0769 (1.86 Å resolution).

Article Snippet: Raw ITC data, DSF data for Biolog assays, GC–MS data, phylogenetic and biogeographical data, and source data for figures are available via the Open Science Framework (10.17605/OSF.IO/47TR5).

Techniques: Comparison, Binding Assay, Software, Titration, Negative Control