Study of molecular interactions with 13C DNP-NMR
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| Title: | Study of molecular interactions with 13C DNP-NMR |
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| Authors: | Lerche, Mathilde H.1 mathilde.lerche@albeda.dk, Meier, Sebastian2, Jensen, Pernille R.1, Baumann, Herbert3, Petersen, Bent O.2, Karlsson, Magnus1, Duus, Jens Ø.2, Ardenkjær-Larsen, Jan H.4 |
| Source: | Journal of Magnetic Resonance. Mar2010, Vol. 203 Issue 1, p52-56. 5p. |
| Subjects: | Molecule-molecule collisions, Nuclear magnetic resonance spectroscopy, Polarization (Nuclear physics), Transients (Dynamics), Ligand binding (Biochemistry), Enzyme inhibitors |
| Abstract: | Abstract: NMR spectroscopy is an established, versatile technique for the detection of molecular interactions, even when these interactions are weak. Signal enhancement by several orders of magnitude through dynamic nuclear polarization alleviates several practical limitations of NMR-based interaction studies. This enhanced non-equilibrium polarization contributes sensitivity for the detection of molecular interactions in a single NMR transient. We show that direct 13C NMR ligand binding studies at natural isotopic abundance of 13C gets feasible in this way. Resultant screens are easy to interpret and can be performed at 13C concentrations below μM. In addition to such ligand-detected studies of molecular interaction, ligand binding can be assessed and quantified with enzymatic assays that employ hyperpolarized substrates at varying enzyme inhibitor concentrations. The physical labeling of nuclear spins by hyperpolarization thus provides the opportunity to devise fast novel in vitro experiments with low material requirement and without the need for synthetic modifications of target or ligands. [Copyright &y& Elsevier] |
| Copyright of Journal of Magnetic Resonance is the property of Academic Press Inc. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) | |
| Database: | Engineering Source |
| FullText | Text: Availability: 0 |
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| Header | DbId: egs DbLabel: Engineering Source An: 47963818 AccessLevel: 6 PubType: Academic Journal PubTypeId: academicJournal PreciseRelevancyScore: 0 |
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| Items | – Name: Title Label: Title Group: Ti Data: Study of molecular interactions with <superscript>13</superscript>C DNP-NMR – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Lerche%2C+Mathilde+H%2E%22">Lerche, Mathilde H.</searchLink><relatesTo>1</relatesTo><i> mathilde.lerche@albeda.dk</i><br /><searchLink fieldCode="AR" term="%22Meier%2C+Sebastian%22">Meier, Sebastian</searchLink><relatesTo>2</relatesTo><br /><searchLink fieldCode="AR" term="%22Jensen%2C+Pernille+R%2E%22">Jensen, Pernille R.</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Baumann%2C+Herbert%22">Baumann, Herbert</searchLink><relatesTo>3</relatesTo><br /><searchLink fieldCode="AR" term="%22Petersen%2C+Bent+O%2E%22">Petersen, Bent O.</searchLink><relatesTo>2</relatesTo><br /><searchLink fieldCode="AR" term="%22Karlsson%2C+Magnus%22">Karlsson, Magnus</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Duus%2C+Jens+Ø%2E%22">Duus, Jens Ø.</searchLink><relatesTo>2</relatesTo><br /><searchLink fieldCode="AR" term="%22Ardenkjær-Larsen%2C+Jan+H%2E%22">Ardenkjær-Larsen, Jan H.</searchLink><relatesTo>4</relatesTo> – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22Journal+of+Magnetic+Resonance%22">Journal of Magnetic Resonance</searchLink>. Mar2010, Vol. 203 Issue 1, p52-56. 5p. – Name: Subject Label: Subjects Group: Su Data: <searchLink fieldCode="DE" term="%22Molecule-molecule+collisions%22">Molecule-molecule collisions</searchLink><br /><searchLink fieldCode="DE" term="%22Nuclear+magnetic+resonance+spectroscopy%22">Nuclear magnetic resonance spectroscopy</searchLink><br /><searchLink fieldCode="DE" term="%22Polarization+%28Nuclear+physics%29%22">Polarization (Nuclear physics)</searchLink><br /><searchLink fieldCode="DE" term="%22Transients+%28Dynamics%29%22">Transients (Dynamics)</searchLink><br /><searchLink fieldCode="DE" term="%22Ligand+binding+%28Biochemistry%29%22">Ligand binding (Biochemistry)</searchLink><br /><searchLink fieldCode="DE" term="%22Enzyme+inhibitors%22">Enzyme inhibitors</searchLink> – Name: Abstract Label: Abstract Group: Ab Data: Abstract: NMR spectroscopy is an established, versatile technique for the detection of molecular interactions, even when these interactions are weak. Signal enhancement by several orders of magnitude through dynamic nuclear polarization alleviates several practical limitations of NMR-based interaction studies. This enhanced non-equilibrium polarization contributes sensitivity for the detection of molecular interactions in a single NMR transient. We show that direct 13C NMR ligand binding studies at natural isotopic abundance of 13C gets feasible in this way. Resultant screens are easy to interpret and can be performed at 13C concentrations below μM. In addition to such ligand-detected studies of molecular interaction, ligand binding can be assessed and quantified with enzymatic assays that employ hyperpolarized substrates at varying enzyme inhibitor concentrations. The physical labeling of nuclear spins by hyperpolarization thus provides the opportunity to devise fast novel in vitro experiments with low material requirement and without the need for synthetic modifications of target or ligands. [Copyright &y& Elsevier] – Name: AbstractSuppliedCopyright Label: Group: Ab Data: <i>Copyright of Journal of Magnetic Resonance is the property of Academic Press Inc. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.) |
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| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.1016/j.jmr.2009.11.020 Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 5 StartPage: 52 Subjects: – SubjectFull: Molecule-molecule collisions Type: general – SubjectFull: Nuclear magnetic resonance spectroscopy Type: general – SubjectFull: Polarization (Nuclear physics) Type: general – SubjectFull: Transients (Dynamics) Type: general – SubjectFull: Ligand binding (Biochemistry) Type: general – SubjectFull: Enzyme inhibitors Type: general Titles: – TitleFull: Study of molecular interactions with 13C DNP-NMR Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Lerche, Mathilde H. – PersonEntity: Name: NameFull: Meier, Sebastian – PersonEntity: Name: NameFull: Jensen, Pernille R. – PersonEntity: Name: NameFull: Baumann, Herbert – PersonEntity: Name: NameFull: Petersen, Bent O. – PersonEntity: Name: NameFull: Karlsson, Magnus – PersonEntity: Name: NameFull: Duus, Jens Ø. – PersonEntity: Name: NameFull: Ardenkjær-Larsen, Jan H. IsPartOfRelationships: – BibEntity: Dates: – D: 01 M: 03 Text: Mar2010 Type: published Y: 2010 Identifiers: – Type: issn-print Value: 10907807 Numbering: – Type: volume Value: 203 – Type: issue Value: 1 Titles: – TitleFull: Journal of Magnetic Resonance Type: main |
| ResultId | 1 |
