An effective intensity-based reference is a cornerstone for quantitative nuclear magnetic resonance (NMR) studies, as the molecular concentration is encoded in its signal. In theory, NMR is well suited for the measurement of competitive protein adsorption onto nanoparticle (NP) surfaces, but current referencing systems are not optimized for multidimensional experiments. Presented herein is a simple and novel referencing system using ^(15)N tryptophan (Trp) as an external reference for ¹H-^(15)N...
[NMR paper] Label-free quantitative 1H NMR spectroscopy to study low-affinity ligand-protein interactions in solution: A contribution to the mechanism of polyphenol-mediated astringency.
Label-free quantitative 1H NMR spectroscopy to study low-affinity ligand-protein interactions in solution: A contribution to the mechanism of polyphenol-mediated astringency.
Label-free quantitative 1H NMR spectroscopy to study low-affinity ligand-protein interactions in solution: A contribution to the mechanism of polyphenol-mediated astringency.
PLoS One. 2017;12(9):e0184487
Authors: Delius J, Frank O, Hofmann T
Abstract
Nuclear magnetic resonance (NMR) spectroscopy is well-established in assessing the binding affinity between...
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09-09-2017 06:59 PM
[NMR paper] Quantitative analysis of protein-ligand interactions by NMR.
Quantitative analysis of protein-ligand interactions by NMR.
Quantitative analysis of protein-ligand interactions by NMR.
Prog Nucl Magn Reson Spectrosc. 2016 Aug;96:47-57
Authors: Furukawa A, Konuma T, Yanaka S, Sugase K
Abstract
Protein-ligand interactions have been commonly studied through static structures of the protein-ligand complex. Recently, however, there has been increasing interest in investigating the dynamics of protein-ligand interactions both for fundamental understanding of the underlying mechanisms and for drug...
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08-31-2016 02:34 PM
Quantitative measurement of exchange dynamics in proteins via 13 C relaxation dispersion of 13 CHD 2 -labeled samples
Quantitative measurement of exchange dynamics in proteins via 13 C relaxation dispersion of 13 CHD 2 -labeled samples
Abstract
Methyl groups have emerged as powerful probes of protein dynamics with timescales from picoseconds to seconds. Typically, studies involving high molecular weight complexes exploit 13CH3- or 13CHD2-labeling in otherwise highly deuterated proteins. The 13CHD2 label offers the unique advantage of providing 13C, 1H and 2H spin probes, however a disadvantage has been the lack of an experiment to record 13C...
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06-02-2016 02:11 AM
[NMR paper] The study of transient protein-nanoparticle interactions by solution NMR spectroscopy.
The study of transient protein-nanoparticle interactions by solution NMR spectroscopy.
Related Articles The study of transient protein-nanoparticle interactions by solution NMR spectroscopy.
Biochim Biophys Acta. 2015 Apr 30;
Authors: Assfalg M, Ragona L, Pagano K, D'Onofrio M, Zanzoni S, Tomaselli S, Molinari H
Abstract
The rapid development of novel nanoscale materials for applications in biomedicine urges an improved characterization of the nano-bio interfaces. Nanoparticles exhibit unique structures and properties, often...
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05-06-2015 11:59 AM
The study of transient protein-nanoparticle interactions by solution NMR spectroscopy
The study of transient protein-nanoparticle interactions by solution NMR spectroscopy
Publication date: Available online 30 April 2015
Source:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics</br>
Author(s): Michael Assfalg , Laura Ragona , Katiuscia Pagano , Mariapina D’Onofrio , Serena Zanzoni , Simona Tomaselli , Henriette Molinari</br>
The rapid development of novel nanoscale materials for applications in biomedicine urges an improved characterization of the nano-bio interfaces. Nanoparticles exhibit unique structures and properties, often...
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04-30-2015 09:13 PM
Ultrafast quantitative 2D NMR: an efficient tool for the measurement of specific isotopic enrichments in complex biological mixtures.
Ultrafast quantitative 2D NMR: an efficient tool for the measurement of specific isotopic enrichments in complex biological mixtures.
Ultrafast quantitative 2D NMR: an efficient tool for the measurement of specific isotopic enrichments in complex biological mixtures.
Anal Chem. 2011 Apr 15;83(8):3112-9
Authors: Giraudeau P, Massou S, Robin Y, Cahoreau E, Portais JC, Akoka S
Two-dimensional nuclear magnetic resonance (2D NMR) is a promising tool for studying metabolic fluxes by measuring (13)C-enrichments in complex mixtures of (13)C-labeled...
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08-04-2011 11:41 AM
Human multiprotein bridging factor 1 and Calmodulin do not interact in vitro as confirmed by NMR spectroscopy and CaM-agarose affinity chromatography.
Human multiprotein bridging factor 1 and Calmodulin do not interact in vitro as confirmed by NMR spectroscopy and CaM-agarose affinity chromatography.
Human multiprotein bridging factor 1 and Calmodulin do not interact in vitro as confirmed by NMR spectroscopy and CaM-agarose affinity chromatography.
Protein Expr Purif. 2011 Jul 14;
Authors: Babini E, Hu X, Parigi G, Vignali M
The human multiprotein bridging factor 1 (hMBF1) has been established in different cellular types to have the role of transcriptional coactivator. It is also reported to be...
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07-26-2011 09:30 PM
[NMR paper] Quantitative measurement of water diffusion lifetimes at a protein/DNA interface by N
Quantitative measurement of water diffusion lifetimes at a protein/DNA interface by NMR.
Related Articles Quantitative measurement of water diffusion lifetimes at a protein/DNA interface by NMR.
J Biomol NMR. 2001 Jun;20(2):111-26
Authors: Gruschus JM, Ferretti JA
Hydration site lifetimes of slowly diffusing water molecules at the protein/DNA interface of the vnd/NK-2 homeodomain DNA complex were determined using novel three-dimensional NMR techniques. The lifetimes were calculated using the ratios of ROE and NOE cross-relaxation rates between...
Quantitative Measurement of Multiprotein Nanoparticle Interactions Using NMR Spectroscopy
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