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<t>ITC</t> traces of CP titrated with CBR126 wt (panel A) or CBR126 mut (panel B). Upper panels are raw traces of thermograms, with differential power for each injection of CBR. Lower panels are binding isotherms, with integrated enthalpy vs molar ratio. Fitted values for K D , with a stoichiometry of one, are listed.
Itc Origin Analysis Software, supplied by Malvern Panalytical, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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<t>ITC</t> traces of CP titrated with CBR126 wt (panel A) or CBR126 mut (panel B). Upper panels are raw traces of thermograms, with differential power for each injection of CBR. Lower panels are binding isotherms, with integrated enthalpy vs molar ratio. Fitted values for K D , with a stoichiometry of one, are listed.
Origin Software Package, supplied by Malvern Panalytical, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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<t>ITC</t> traces of CP titrated with CBR126 wt (panel A) or CBR126 mut (panel B). Upper panels are raw traces of thermograms, with differential power for each injection of CBR. Lower panels are binding isotherms, with integrated enthalpy vs molar ratio. Fitted values for K D , with a stoichiometry of one, are listed.
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<t>ITC</t> traces of CP titrated with CBR126 wt (panel A) or CBR126 mut (panel B). Upper panels are raw traces of thermograms, with differential power for each injection of CBR. Lower panels are binding isotherms, with integrated enthalpy vs molar ratio. Fitted values for K D , with a stoichiometry of one, are listed.
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a , Modified click reaction 25 to make Cbl derivatives from 58 using a variable azide. b , Simplified chemical structures of Cbls 63 - 65 that were made to systematically test our design hypotheses. c , Fluorescence displacement binding curve for CNCbl and 63 - 65 shown as mean and s.e.m. from independent experiments ( n = 4 except for data from CNCbl where n = 3). K D values are reported as mean and s.d. from independent experiments ( n = 4 except for data from CNCbl where n = 3). d , To verify the near-picomolar binding of 63 and 64 , we used <t>ITC</t> with the env8 aptamer domain. Given that this RNA shows weaker ligand binding than the full-length env8 , 19 it is in the perfect regime for ITC. Representative ITC binding isotherm for the env8 aptamer domain with CNCbl, 63 , and 64 . e , Co-crystal structure of env2 -Cbl 63 showing only the binding pocket nucleotides and the β-axial group. Proposed hydrogen bonds, which are weakly supported by the electron density, are shown as double arrows. All mesh representations correspond to a simulated annealing 2F o -F c map where A20 and the ligand were omitted from the model and are shown at 1 σ contour. f , Same as in e but for env2 -Cbl 64 . g , Fold repression for our reporter system in the presence of CNCbl and 63 - 65 and for cells with CNCbl and excess amounts of 63 - 65 added. Mean and s.d. from biological replicates ( n = 4) are shown. For comparison, the mean fold repression of 10 nM CNCbl is shown as a dashed line its s.d. is represented as a shaded box. h , Simplified chemical structure of the titratable pyridine Cbl 66 . i , Representative ITC binding isotherms for env8 aptamer domain with CNCbl, 29 , and 66 at pH 8 and pH 5. For all ITC data, K D values are reported as mean and s.d. from independent experiments ( n = 3).
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ITC traces of CP titrated with CBR126 wt (panel A) or CBR126 mut (panel B). Upper panels are raw traces of thermograms, with differential power for each injection of CBR. Lower panels are binding isotherms, with integrated enthalpy vs molar ratio. Fitted values for K D , with a stoichiometry of one, are listed.

Journal: bioRxiv

Article Title: Biochemical Functions of the Membrane-Binding Domain of CARMIL

doi: 10.64898/2026.01.05.697744

Figure Lengend Snippet: ITC traces of CP titrated with CBR126 wt (panel A) or CBR126 mut (panel B). Upper panels are raw traces of thermograms, with differential power for each injection of CBR. Lower panels are binding isotherms, with integrated enthalpy vs molar ratio. Fitted values for K D , with a stoichiometry of one, are listed.

Article Snippet: Binding constants were determined by fitting the change in enthalpy to a single site binding model using MicroCal ITC Origin analysis software.

Techniques: Injection, Binding Assay

a , Modified click reaction 25 to make Cbl derivatives from 58 using a variable azide. b , Simplified chemical structures of Cbls 63 - 65 that were made to systematically test our design hypotheses. c , Fluorescence displacement binding curve for CNCbl and 63 - 65 shown as mean and s.e.m. from independent experiments ( n = 4 except for data from CNCbl where n = 3). K D values are reported as mean and s.d. from independent experiments ( n = 4 except for data from CNCbl where n = 3). d , To verify the near-picomolar binding of 63 and 64 , we used ITC with the env8 aptamer domain. Given that this RNA shows weaker ligand binding than the full-length env8 , 19 it is in the perfect regime for ITC. Representative ITC binding isotherm for the env8 aptamer domain with CNCbl, 63 , and 64 . e , Co-crystal structure of env2 -Cbl 63 showing only the binding pocket nucleotides and the β-axial group. Proposed hydrogen bonds, which are weakly supported by the electron density, are shown as double arrows. All mesh representations correspond to a simulated annealing 2F o -F c map where A20 and the ligand were omitted from the model and are shown at 1 σ contour. f , Same as in e but for env2 -Cbl 64 . g , Fold repression for our reporter system in the presence of CNCbl and 63 - 65 and for cells with CNCbl and excess amounts of 63 - 65 added. Mean and s.d. from biological replicates ( n = 4) are shown. For comparison, the mean fold repression of 10 nM CNCbl is shown as a dashed line its s.d. is represented as a shaded box. h , Simplified chemical structure of the titratable pyridine Cbl 66 . i , Representative ITC binding isotherms for env8 aptamer domain with CNCbl, 29 , and 66 at pH 8 and pH 5. For all ITC data, K D values are reported as mean and s.d. from independent experiments ( n = 3).

Journal: Nature chemical biology

Article Title: Designing small molecules targeting a cryptic RNA binding site via base displacement

doi: 10.1038/s41589-025-02018-8

Figure Lengend Snippet: a , Modified click reaction 25 to make Cbl derivatives from 58 using a variable azide. b , Simplified chemical structures of Cbls 63 - 65 that were made to systematically test our design hypotheses. c , Fluorescence displacement binding curve for CNCbl and 63 - 65 shown as mean and s.e.m. from independent experiments ( n = 4 except for data from CNCbl where n = 3). K D values are reported as mean and s.d. from independent experiments ( n = 4 except for data from CNCbl where n = 3). d , To verify the near-picomolar binding of 63 and 64 , we used ITC with the env8 aptamer domain. Given that this RNA shows weaker ligand binding than the full-length env8 , 19 it is in the perfect regime for ITC. Representative ITC binding isotherm for the env8 aptamer domain with CNCbl, 63 , and 64 . e , Co-crystal structure of env2 -Cbl 63 showing only the binding pocket nucleotides and the β-axial group. Proposed hydrogen bonds, which are weakly supported by the electron density, are shown as double arrows. All mesh representations correspond to a simulated annealing 2F o -F c map where A20 and the ligand were omitted from the model and are shown at 1 σ contour. f , Same as in e but for env2 -Cbl 64 . g , Fold repression for our reporter system in the presence of CNCbl and 63 - 65 and for cells with CNCbl and excess amounts of 63 - 65 added. Mean and s.d. from biological replicates ( n = 4) are shown. For comparison, the mean fold repression of 10 nM CNCbl is shown as a dashed line its s.d. is represented as a shaded box. h , Simplified chemical structure of the titratable pyridine Cbl 66 . i , Representative ITC binding isotherms for env8 aptamer domain with CNCbl, 29 , and 66 at pH 8 and pH 5. For all ITC data, K D values are reported as mean and s.d. from independent experiments ( n = 3).

Article Snippet: Data were fit to a single-site binding model using Origin 7 ITC software (MicroCal).

Techniques: Modification, Fluorescence, Binding Assay, Ligand Binding Assay, Comparison