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itc software  (OriginLab corp)


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    Structured Review

    OriginLab corp itc software
    Itc Software, 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
    https://www.bioz.com/product/itc+origin+analysis+software/itc+data+analysis+software/pmc07914709-91-5-7
    Average 90 stars, based on 1 article reviews
    itc software - by Bioz Stars, 2026-11
    90/100 stars

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    Related Articles

    other:

    Article Title: Crystal structure and conformational stability of a galectin-1 tandem-repeat mutant with a short linker.
    Article Snippet: Modification of the domain architecture of galectins has been attempted to analyze their biological functions and to develop medical applications.. Several types of galectin-1 repeat mutants were previously reported but, however, it was not clear whether the native structure of the wild type was retained.. In this study, we determined the crystal structure of a galectin-1 tandem-repeat mutant with a short linker peptide, and compared the unfolding profiles of the wild type and mutant by chemical denaturation.

    Article Title: Characterization of Type1 Lipid Transfer Protein from Citrus sinensis: Unraveling its potential as an antimicrobial and insecticidal agent.
    Article Snippet: Lipid Transfer Protein1 (LTP1) is a cationic, multifaceted protein belonging to the pathogenesis-related protein (PR14) family.. Despite being involved in diverse physiological processes and defense mechanisms, the precise invivo role of LTP1 remains undiscovered.. This work presents the characterization of recombinant Citrus sinensis LTP1 (CsLTP1) along with lipid binding studies through in-silico and in-vitro approaches.

    Article Title: Insights on autophagosome–lysosome tethering from structural and biochemical characterization of human autophagy factor EPG5
    Article Snippet: The ITC data were analyzed with one-site binding model using Origin 7.0 (OriginLab).

    Article Title: A transient conformation facilitates ligand binding to the adenine riboswitch
    Article Snippet: ITC experiments of the RNA samples were performed in a buffer containing 10 mM HEPES, 100 mM KCl, 10 mM MgCl 2 , pH 7.5, using a MicroCal ITC200 calorimeter (General Electric, USA).

    Software:

    Article Title: Observation of structural switch in nascent SAM-VI riboswitch during transcription at single-nucleotide and single-molecule resolution.
    Article Snippet: .. The ITCdata subtracted backgroundwasfitted by a one-site bindingmodel using Origin ITC software (OriginLab, USA). .. Steady-state fluorescence experiments for 2AP-riboSAM and 2APmutant upon titration of SAM were conducted on a FLS 1000 photoluminescence spectrometer (Edinburgh Instruments Ltd., UK) at room temperature.

    Article Title: Observation of structural switch in nascent SAM-VI riboswitch during transcription at single-nucleotide and single-molecule resolution
    Article Snippet: .. The ITC data subtracted background was fitted by a one-site binding model using Origin ITC software (OriginLab, USA). .. Steady-state fluorescence experiments for 2AP-riboSAM and 2AP-mutant upon titration of SAM were conducted on a FLS 1000 photoluminescence spectrometer (Edinburgh Instruments Ltd., UK) at room temperature.

    Article Title: Structural basis of terephthalate recognition by solute binding protein TphC
    Article Snippet: .. The resulting data were processed and an independent binding model was fit in ITC data analysis software (OriginLab Corporation). ..

    Binding Assay:

    Article Title: Observation of structural switch in nascent SAM-VI riboswitch during transcription at single-nucleotide and single-molecule resolution
    Article Snippet: .. The ITC data subtracted background was fitted by a one-site binding model using Origin ITC software (OriginLab, USA). .. Steady-state fluorescence experiments for 2AP-riboSAM and 2AP-mutant upon titration of SAM were conducted on a FLS 1000 photoluminescence spectrometer (Edinburgh Instruments Ltd., UK) at room temperature.

    Article Title: Structural basis of terephthalate recognition by solute binding protein TphC
    Article Snippet: .. The resulting data were processed and an independent binding model was fit in ITC data analysis software (OriginLab Corporation). ..



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    Image Search Results


    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

    H3Q5ser stabilizes Taf3-PHD/H3K4me2 and Taf3-PHD/H3K4me3 complexes. ( A ) Experimental (blue) and fitted (red) spectra of free, ∼50% bound, and fully bound TAF3-PHD resonances E862 and C896 for H3K4me3/H3K4me3Q5ser complex. Transfer peaks indicated with *. Experimental spectrum of E862 is also shown separately for clarity. ( B ) ITC analysis of GST-tagged Taf3-PHD binding to H3K4me3 in yellow and H3K4me3Q5ser in navy blue. Top panel displays the raw heat change per injection of H3 peptide. Bottom panel represents the binding isotherm. The solid line represents the best fit to the one-set-of-sites model using MicroCal-ITC Origin 7 software.

    Journal: Nucleic Acids Research

    Article Title: Molecular determinants for recognition of serotonylated chromatin

    doi: 10.1093/nar/gkaf612

    Figure Lengend Snippet: H3Q5ser stabilizes Taf3-PHD/H3K4me2 and Taf3-PHD/H3K4me3 complexes. ( A ) Experimental (blue) and fitted (red) spectra of free, ∼50% bound, and fully bound TAF3-PHD resonances E862 and C896 for H3K4me3/H3K4me3Q5ser complex. Transfer peaks indicated with *. Experimental spectrum of E862 is also shown separately for clarity. ( B ) ITC analysis of GST-tagged Taf3-PHD binding to H3K4me3 in yellow and H3K4me3Q5ser in navy blue. Top panel displays the raw heat change per injection of H3 peptide. Bottom panel represents the binding isotherm. The solid line represents the best fit to the one-set-of-sites model using MicroCal-ITC Origin 7 software.

    Article Snippet: ITC data were subsequently analysed and fitted with the one-site binding model in the MicroCal ITC Origin Analysis software 7.0 (Table , Figs and , , and ).

    Techniques: Binding Assay, Injection, Software

    Taf3-PHD P881 and W894 form key interaction surface with the serotonin group. ( A ) ITC analysis of GST-tagged Taf3-PHD mutants, BPTF-PHD , PHF2-PHD, or PHF8-PHD with the peptides H3K4me3 (in yellow) and H3K4me3Q5ser (in blue). Top panels display the raw heat change per injection of H3 peptide. Bottom panels represent the binding isotherm. The solid line represents the best fit to the one-set-of-sites model using MicroCal-ITC Origin 7 software. ( B ) Multiple sequence alignment (MSA) of human PHD fingers for which high-resolution structures in complex with H3K4me3 are available (ASH1L PDB: 8VLF; BPTF(2) PDB: 2FUU; DIDO1 PDB: 4L7X; ING1 PDB: 2QIC; ING4 PDB: 2PNX/2VNF; ING5 PDB: 3C6W; KMT2E PDB: 4L58; PHF2 PDB: 3KQI; PHF13 PDB: 3O7A; UHRF1 PDB: 3SOW). Consensus Cys4–His–Cys3 positions are highlighted in grey and indicated on top. Locations of the secondary structure elements of TAF3-PHD are indicated on top. S880 and A902 are highlighted in purple, while P881 and W894 are highlighted in yellow.

    Journal: Nucleic Acids Research

    Article Title: Molecular determinants for recognition of serotonylated chromatin

    doi: 10.1093/nar/gkaf612

    Figure Lengend Snippet: Taf3-PHD P881 and W894 form key interaction surface with the serotonin group. ( A ) ITC analysis of GST-tagged Taf3-PHD mutants, BPTF-PHD , PHF2-PHD, or PHF8-PHD with the peptides H3K4me3 (in yellow) and H3K4me3Q5ser (in blue). Top panels display the raw heat change per injection of H3 peptide. Bottom panels represent the binding isotherm. The solid line represents the best fit to the one-set-of-sites model using MicroCal-ITC Origin 7 software. ( B ) Multiple sequence alignment (MSA) of human PHD fingers for which high-resolution structures in complex with H3K4me3 are available (ASH1L PDB: 8VLF; BPTF(2) PDB: 2FUU; DIDO1 PDB: 4L7X; ING1 PDB: 2QIC; ING4 PDB: 2PNX/2VNF; ING5 PDB: 3C6W; KMT2E PDB: 4L58; PHF2 PDB: 3KQI; PHF13 PDB: 3O7A; UHRF1 PDB: 3SOW). Consensus Cys4–His–Cys3 positions are highlighted in grey and indicated on top. Locations of the secondary structure elements of TAF3-PHD are indicated on top. S880 and A902 are highlighted in purple, while P881 and W894 are highlighted in yellow.

    Article Snippet: ITC data were subsequently analysed and fitted with the one-site binding model in the MicroCal ITC Origin Analysis software 7.0 (Table , Figs and , , and ).

    Techniques: Injection, Binding Assay, Software, Sequencing