prism 5·03 Search Results


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In vitro folded Y 2 R variants functionally activate purified G i protein. (A) Y 2 R folded into isotropic bicelles and activated with NPY drastically accelerates nucleotide exchange of wild type Gα i1 . The fluorescence trace is given as mean of seven independent experiments. (B) Resulting apparent rates of GTPγS binding of Gα i1 (basal) and Y 2 R-catalyzed nucleotide exchange. Statistical significance was determined using one-way ANOVA/Dunnett's post hoc test against basal Gα i1 in Graph Pad Prism 5.03. ### p < 0.001; ## p < 0.01.
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In vitro folded Y 2 R variants functionally activate purified G i protein. (A) Y 2 R folded into isotropic bicelles and activated with NPY drastically accelerates nucleotide exchange of wild type Gα i1 . The fluorescence trace is given as mean of seven independent experiments. (B) Resulting apparent rates of GTPγS binding of Gα i1 (basal) and Y 2 R-catalyzed nucleotide exchange. Statistical significance was determined using one-way ANOVA/Dunnett's post hoc test against basal Gα i1 in Graph Pad Prism 5.03. ### p < 0.001; ## p < 0.01.
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In vitro folded Y 2 R variants functionally activate purified G i protein. (A) Y 2 R folded into isotropic bicelles and activated with NPY drastically accelerates nucleotide exchange of wild type Gα i1 . The fluorescence trace is given as mean of seven independent experiments. (B) Resulting apparent rates of GTPγS binding of Gα i1 (basal) and Y 2 R-catalyzed nucleotide exchange. Statistical significance was determined using one-way ANOVA/Dunnett's post hoc test against basal Gα i1 in Graph Pad Prism 5.03. ### p < 0.001; ## p < 0.01.
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In vitro folded Y 2 R variants functionally activate purified G i protein. (A) Y 2 R folded into isotropic bicelles and activated with NPY drastically accelerates nucleotide exchange of wild type Gα i1 . The fluorescence trace is given as mean of seven independent experiments. (B) Resulting apparent rates of GTPγS binding of Gα i1 (basal) and Y 2 R-catalyzed nucleotide exchange. Statistical significance was determined using one-way ANOVA/Dunnett's post hoc test against basal Gα i1 in Graph Pad Prism 5.03. ### p < 0.001; ## p < 0.01.
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In vitro folded Y 2 R variants functionally activate purified G i protein. (A) Y 2 R folded into isotropic bicelles and activated with NPY drastically accelerates nucleotide exchange of wild type Gα i1 . The fluorescence trace is given as mean of seven independent experiments. (B) Resulting apparent rates of GTPγS binding of Gα i1 (basal) and Y 2 R-catalyzed nucleotide exchange. Statistical significance was determined using one-way ANOVA/Dunnett's post hoc test against basal Gα i1 in Graph Pad Prism 5.03. ### p < 0.001; ## p < 0.01.
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In vitro folded Y 2 R variants functionally activate purified G i protein. (A) Y 2 R folded into isotropic bicelles and activated with NPY drastically accelerates nucleotide exchange of wild type Gα i1 . The fluorescence trace is given as mean of seven independent experiments. (B) Resulting apparent rates of GTPγS binding of Gα i1 (basal) and Y 2 R-catalyzed nucleotide exchange. Statistical significance was determined using one-way ANOVA/Dunnett's post hoc test against basal Gα i1 in Graph Pad Prism 5.03. ### p < 0.001; ## p < 0.01.

Journal: Frontiers in Molecular Biosciences

Article Title: Improved in Vitro Folding of the Y 2 G Protein-Coupled Receptor into Bicelles

doi: 10.3389/fmolb.2017.00100

Figure Lengend Snippet: In vitro folded Y 2 R variants functionally activate purified G i protein. (A) Y 2 R folded into isotropic bicelles and activated with NPY drastically accelerates nucleotide exchange of wild type Gα i1 . The fluorescence trace is given as mean of seven independent experiments. (B) Resulting apparent rates of GTPγS binding of Gα i1 (basal) and Y 2 R-catalyzed nucleotide exchange. Statistical significance was determined using one-way ANOVA/Dunnett's post hoc test against basal Gα i1 in Graph Pad Prism 5.03. ### p < 0.001; ## p < 0.01.

Article Snippet: GTPγS binding kinetics was fitted applying the built-in one-phase association function of GraphPad Prism 5.03 (GraphPad Software, San Diego, CA, USA) to obtain the apparent rate constant k.

Techniques: In Vitro, Purification, Fluorescence, Binding Assay