Geometric features of the Wiseman isotherm in isothermal titration calorimetry
Abstract Isothermal titration calorimetry (ITC) has become a standard and preferred technique for studying intermolecular interactions. ITC is the only technique that allows determining the binding affinity, the binding enthalpy, and the stoichiometry in a single experiment. With a practical window...
Ausführliche Beschreibung
Autor*in: |
Velazquez-Campoy, Adrian [verfasserIn] |
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Sprache: |
Englisch |
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2015 |
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Anmerkung: |
© Akadémiai Kiadó, Budapest, Hungary 2015 |
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Übergeordnetes Werk: |
Enthalten in: Journal of thermal analysis and calorimetry - Springer Netherlands, 1998, 122(2015), 3 vom: 02. Juli, Seite 1477-1483 |
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Übergeordnetes Werk: |
volume:122 ; year:2015 ; number:3 ; day:02 ; month:07 ; pages:1477-1483 |
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DOI / URN: |
10.1007/s10973-015-4775-x |
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OLC2049841094 |
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10.1007/s10973-015-4775-x doi (DE-627)OLC2049841094 (DE-He213)s10973-015-4775-x-p DE-627 ger DE-627 rakwb eng 660 VZ Velazquez-Campoy, Adrian verfasserin aut Geometric features of the Wiseman isotherm in isothermal titration calorimetry 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Akadémiai Kiadó, Budapest, Hungary 2015 Abstract Isothermal titration calorimetry (ITC) has become a standard and preferred technique for studying intermolecular interactions. ITC is the only technique that allows determining the binding affinity, the binding enthalpy, and the stoichiometry in a single experiment. With a practical window of more than five orders of magnitude for reliable binding affinity determination (Kd range from millimolar to nanomolar) and its high sensitivity for measuring small heats of reaction (<1 µJ), it is especially suited for characterizing non-covalent interactions typical from biomacromolecular interactions. The Wiseman isotherm represents the usual way of presenting and analyzing the calorimetric binding data. A geometric analysis of the binding isotherm reveals important connections between certain geometric points in the isotherm and the binding parameters. Thus, although the binding parameters (in particular, affinity and enthalpy) must always be estimated through nonlinear analysis of the binding isotherm, it is also possible to easily obtain estimates of those binding parameters through the relationships presented in this work. Isothermal titration calorimetry Binding isotherm Geometric analysis Binding affinity Binding enthalpy Enthalten in Journal of thermal analysis and calorimetry Springer Netherlands, 1998 122(2015), 3 vom: 02. Juli, Seite 1477-1483 (DE-627)244148767 (DE-600)1429493-X (DE-576)066397693 1388-6150 nnns volume:122 year:2015 number:3 day:02 month:07 pages:1477-1483 https://doi.org/10.1007/s10973-015-4775-x lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE GBV_ILN_70 AR 122 2015 3 02 07 1477-1483 |
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10.1007/s10973-015-4775-x doi (DE-627)OLC2049841094 (DE-He213)s10973-015-4775-x-p DE-627 ger DE-627 rakwb eng 660 VZ Velazquez-Campoy, Adrian verfasserin aut Geometric features of the Wiseman isotherm in isothermal titration calorimetry 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Akadémiai Kiadó, Budapest, Hungary 2015 Abstract Isothermal titration calorimetry (ITC) has become a standard and preferred technique for studying intermolecular interactions. ITC is the only technique that allows determining the binding affinity, the binding enthalpy, and the stoichiometry in a single experiment. With a practical window of more than five orders of magnitude for reliable binding affinity determination (Kd range from millimolar to nanomolar) and its high sensitivity for measuring small heats of reaction (<1 µJ), it is especially suited for characterizing non-covalent interactions typical from biomacromolecular interactions. The Wiseman isotherm represents the usual way of presenting and analyzing the calorimetric binding data. A geometric analysis of the binding isotherm reveals important connections between certain geometric points in the isotherm and the binding parameters. Thus, although the binding parameters (in particular, affinity and enthalpy) must always be estimated through nonlinear analysis of the binding isotherm, it is also possible to easily obtain estimates of those binding parameters through the relationships presented in this work. Isothermal titration calorimetry Binding isotherm Geometric analysis Binding affinity Binding enthalpy Enthalten in Journal of thermal analysis and calorimetry Springer Netherlands, 1998 122(2015), 3 vom: 02. Juli, Seite 1477-1483 (DE-627)244148767 (DE-600)1429493-X (DE-576)066397693 1388-6150 nnns volume:122 year:2015 number:3 day:02 month:07 pages:1477-1483 https://doi.org/10.1007/s10973-015-4775-x lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE GBV_ILN_70 AR 122 2015 3 02 07 1477-1483 |
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10.1007/s10973-015-4775-x doi (DE-627)OLC2049841094 (DE-He213)s10973-015-4775-x-p DE-627 ger DE-627 rakwb eng 660 VZ Velazquez-Campoy, Adrian verfasserin aut Geometric features of the Wiseman isotherm in isothermal titration calorimetry 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Akadémiai Kiadó, Budapest, Hungary 2015 Abstract Isothermal titration calorimetry (ITC) has become a standard and preferred technique for studying intermolecular interactions. ITC is the only technique that allows determining the binding affinity, the binding enthalpy, and the stoichiometry in a single experiment. With a practical window of more than five orders of magnitude for reliable binding affinity determination (Kd range from millimolar to nanomolar) and its high sensitivity for measuring small heats of reaction (<1 µJ), it is especially suited for characterizing non-covalent interactions typical from biomacromolecular interactions. The Wiseman isotherm represents the usual way of presenting and analyzing the calorimetric binding data. A geometric analysis of the binding isotherm reveals important connections between certain geometric points in the isotherm and the binding parameters. Thus, although the binding parameters (in particular, affinity and enthalpy) must always be estimated through nonlinear analysis of the binding isotherm, it is also possible to easily obtain estimates of those binding parameters through the relationships presented in this work. Isothermal titration calorimetry Binding isotherm Geometric analysis Binding affinity Binding enthalpy Enthalten in Journal of thermal analysis and calorimetry Springer Netherlands, 1998 122(2015), 3 vom: 02. Juli, Seite 1477-1483 (DE-627)244148767 (DE-600)1429493-X (DE-576)066397693 1388-6150 nnns volume:122 year:2015 number:3 day:02 month:07 pages:1477-1483 https://doi.org/10.1007/s10973-015-4775-x lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE GBV_ILN_70 AR 122 2015 3 02 07 1477-1483 |
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10.1007/s10973-015-4775-x doi (DE-627)OLC2049841094 (DE-He213)s10973-015-4775-x-p DE-627 ger DE-627 rakwb eng 660 VZ Velazquez-Campoy, Adrian verfasserin aut Geometric features of the Wiseman isotherm in isothermal titration calorimetry 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Akadémiai Kiadó, Budapest, Hungary 2015 Abstract Isothermal titration calorimetry (ITC) has become a standard and preferred technique for studying intermolecular interactions. ITC is the only technique that allows determining the binding affinity, the binding enthalpy, and the stoichiometry in a single experiment. With a practical window of more than five orders of magnitude for reliable binding affinity determination (Kd range from millimolar to nanomolar) and its high sensitivity for measuring small heats of reaction (<1 µJ), it is especially suited for characterizing non-covalent interactions typical from biomacromolecular interactions. The Wiseman isotherm represents the usual way of presenting and analyzing the calorimetric binding data. A geometric analysis of the binding isotherm reveals important connections between certain geometric points in the isotherm and the binding parameters. Thus, although the binding parameters (in particular, affinity and enthalpy) must always be estimated through nonlinear analysis of the binding isotherm, it is also possible to easily obtain estimates of those binding parameters through the relationships presented in this work. Isothermal titration calorimetry Binding isotherm Geometric analysis Binding affinity Binding enthalpy Enthalten in Journal of thermal analysis and calorimetry Springer Netherlands, 1998 122(2015), 3 vom: 02. Juli, Seite 1477-1483 (DE-627)244148767 (DE-600)1429493-X (DE-576)066397693 1388-6150 nnns volume:122 year:2015 number:3 day:02 month:07 pages:1477-1483 https://doi.org/10.1007/s10973-015-4775-x lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE GBV_ILN_70 AR 122 2015 3 02 07 1477-1483 |
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10.1007/s10973-015-4775-x doi (DE-627)OLC2049841094 (DE-He213)s10973-015-4775-x-p DE-627 ger DE-627 rakwb eng 660 VZ Velazquez-Campoy, Adrian verfasserin aut Geometric features of the Wiseman isotherm in isothermal titration calorimetry 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Akadémiai Kiadó, Budapest, Hungary 2015 Abstract Isothermal titration calorimetry (ITC) has become a standard and preferred technique for studying intermolecular interactions. ITC is the only technique that allows determining the binding affinity, the binding enthalpy, and the stoichiometry in a single experiment. With a practical window of more than five orders of magnitude for reliable binding affinity determination (Kd range from millimolar to nanomolar) and its high sensitivity for measuring small heats of reaction (<1 µJ), it is especially suited for characterizing non-covalent interactions typical from biomacromolecular interactions. The Wiseman isotherm represents the usual way of presenting and analyzing the calorimetric binding data. A geometric analysis of the binding isotherm reveals important connections between certain geometric points in the isotherm and the binding parameters. Thus, although the binding parameters (in particular, affinity and enthalpy) must always be estimated through nonlinear analysis of the binding isotherm, it is also possible to easily obtain estimates of those binding parameters through the relationships presented in this work. Isothermal titration calorimetry Binding isotherm Geometric analysis Binding affinity Binding enthalpy Enthalten in Journal of thermal analysis and calorimetry Springer Netherlands, 1998 122(2015), 3 vom: 02. Juli, Seite 1477-1483 (DE-627)244148767 (DE-600)1429493-X (DE-576)066397693 1388-6150 nnns volume:122 year:2015 number:3 day:02 month:07 pages:1477-1483 https://doi.org/10.1007/s10973-015-4775-x lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE GBV_ILN_70 AR 122 2015 3 02 07 1477-1483 |
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Abstract Isothermal titration calorimetry (ITC) has become a standard and preferred technique for studying intermolecular interactions. ITC is the only technique that allows determining the binding affinity, the binding enthalpy, and the stoichiometry in a single experiment. With a practical window of more than five orders of magnitude for reliable binding affinity determination (Kd range from millimolar to nanomolar) and its high sensitivity for measuring small heats of reaction (<1 µJ), it is especially suited for characterizing non-covalent interactions typical from biomacromolecular interactions. The Wiseman isotherm represents the usual way of presenting and analyzing the calorimetric binding data. A geometric analysis of the binding isotherm reveals important connections between certain geometric points in the isotherm and the binding parameters. Thus, although the binding parameters (in particular, affinity and enthalpy) must always be estimated through nonlinear analysis of the binding isotherm, it is also possible to easily obtain estimates of those binding parameters through the relationships presented in this work. © Akadémiai Kiadó, Budapest, Hungary 2015 |
abstractGer |
Abstract Isothermal titration calorimetry (ITC) has become a standard and preferred technique for studying intermolecular interactions. ITC is the only technique that allows determining the binding affinity, the binding enthalpy, and the stoichiometry in a single experiment. With a practical window of more than five orders of magnitude for reliable binding affinity determination (Kd range from millimolar to nanomolar) and its high sensitivity for measuring small heats of reaction (<1 µJ), it is especially suited for characterizing non-covalent interactions typical from biomacromolecular interactions. The Wiseman isotherm represents the usual way of presenting and analyzing the calorimetric binding data. A geometric analysis of the binding isotherm reveals important connections between certain geometric points in the isotherm and the binding parameters. Thus, although the binding parameters (in particular, affinity and enthalpy) must always be estimated through nonlinear analysis of the binding isotherm, it is also possible to easily obtain estimates of those binding parameters through the relationships presented in this work. © Akadémiai Kiadó, Budapest, Hungary 2015 |
abstract_unstemmed |
Abstract Isothermal titration calorimetry (ITC) has become a standard and preferred technique for studying intermolecular interactions. ITC is the only technique that allows determining the binding affinity, the binding enthalpy, and the stoichiometry in a single experiment. With a practical window of more than five orders of magnitude for reliable binding affinity determination (Kd range from millimolar to nanomolar) and its high sensitivity for measuring small heats of reaction (<1 µJ), it is especially suited for characterizing non-covalent interactions typical from biomacromolecular interactions. The Wiseman isotherm represents the usual way of presenting and analyzing the calorimetric binding data. A geometric analysis of the binding isotherm reveals important connections between certain geometric points in the isotherm and the binding parameters. Thus, although the binding parameters (in particular, affinity and enthalpy) must always be estimated through nonlinear analysis of the binding isotherm, it is also possible to easily obtain estimates of those binding parameters through the relationships presented in this work. © Akadémiai Kiadó, Budapest, Hungary 2015 |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">OLC2049841094</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230503170102.0</controlfield><controlfield tag="007">tu</controlfield><controlfield tag="008">200820s2015 xx ||||| 00| ||eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1007/s10973-015-4775-x</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)OLC2049841094</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-He213)s10973-015-4775-x-p</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="082" ind1="0" ind2="4"><subfield code="a">660</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Velazquez-Campoy, Adrian</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Geometric features of the Wiseman isotherm in isothermal titration calorimetry</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2015</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">ohne Hilfsmittel zu benutzen</subfield><subfield code="b">n</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Band</subfield><subfield code="b">nc</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="500" ind1=" " ind2=" "><subfield code="a">© Akadémiai Kiadó, Budapest, Hungary 2015</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Abstract Isothermal titration calorimetry (ITC) has become a standard and preferred technique for studying intermolecular interactions. ITC is the only technique that allows determining the binding affinity, the binding enthalpy, and the stoichiometry in a single experiment. With a practical window of more than five orders of magnitude for reliable binding affinity determination (Kd range from millimolar to nanomolar) and its high sensitivity for measuring small heats of reaction (<1 µJ), it is especially suited for characterizing non-covalent interactions typical from biomacromolecular interactions. The Wiseman isotherm represents the usual way of presenting and analyzing the calorimetric binding data. A geometric analysis of the binding isotherm reveals important connections between certain geometric points in the isotherm and the binding parameters. Thus, although the binding parameters (in particular, affinity and enthalpy) must always be estimated through nonlinear analysis of the binding isotherm, it is also possible to easily obtain estimates of those binding parameters through the relationships presented in this work.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Isothermal titration calorimetry</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Binding isotherm</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Geometric analysis</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Binding affinity</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Binding enthalpy</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="t">Journal of thermal analysis and calorimetry</subfield><subfield code="d">Springer Netherlands, 1998</subfield><subfield code="g">122(2015), 3 vom: 02. 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