[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
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] Structural Basis for TatA Oligomerization: An NMR Study of Escherichia coli TatA Dimeric Structure.
Structural Basis for TatA Oligomerization: An NMR Study of Escherichia coli TatA Dimeric Structure.
Related Articles Structural Basis for TatA Oligomerization: An NMR Study of Escherichia coli TatA Dimeric Structure.
PLoS One. 2014;9(8):e103157
Authors: Zhang Y, Hu Y, Li H, Jin C
Abstract
Many proteins are transported across lipid membranes by protein translocation systems in living cells. The twin-arginine transport (Tat) system identified in bacteria and plant chloroplasts is a unique system that transports proteins across...
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08-05-2014 04:47 PM
Journal Highlight: Quantitative NMR: An applicable method for quantitative analysis of medicinal plant extracts and herbal products
Journal Highlight: Quantitative NMR: An applicable method for quantitative analysis of medicinal plant extracts and herbal products
http://www.spectroscopynow.com/common/images/thumbnails/13abcca009b.jpgA quantitative NMR method has been reported for quantitative analysis of three medicinal plant extracts and their herbal products without the need of authentic standards.
Source: Spectroscopynow.com
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02-03-2013 08:49 AM
Conformational analysis by quantitative NOE measurements of the β-proton pairs across individual disulfide bonds in proteins
Conformational analysis by quantitative NOE measurements of the β-proton pairs across individual disulfide bonds in proteins
Abstract NOEs between the β-protons of cysteine residues across disulfide bonds in proteins provide direct information on the connectivities and conformations of these important cross-links, which are otherwise difficult to investigate. With conventional -proteins, however, fast spin diffusion processes mediated by strong dipolar interactions between geminal β-protons prohibit the quantitative measurements and thus the analyses of long-range NOEs across...
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12-05-2011 04:07 AM
[NMR paper] Quantitative NMR studies of high molecular weight proteins: application to domain ori
Quantitative NMR studies of high molecular weight proteins: application to domain orientation and ligand binding in the 723 residue enzyme malate synthase G.
Related Articles Quantitative NMR studies of high molecular weight proteins: application to domain orientation and ligand binding in the 723 residue enzyme malate synthase G.
J Mol Biol. 2003 Apr 11;327(5):1121-33
Authors: Tugarinov V, Kay LE
A high-resolution multidimensional NMR study of ligand-binding to Escherichia coli malate synthase G (MSG), a 723-residue monomeric enzyme (81.4...
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11-24-2010 09:01 PM
[NMR paper] Oligomerization of the EGF receptor transmembrane domain: a 2H NMR study in lipid bil
Oligomerization of the EGF receptor transmembrane domain: a 2H NMR study in lipid bilayers.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Oligomerization of the EGF receptor transmembrane domain: a 2H NMR study in lipid bilayers.
Biochemistry. 1997 Oct 14;36(41):12616-24
Authors: Jones DH, Rigby AC, Barber KR, Grant CW
During the course of a previous study by wideline 2H NMR, we noted spectral features suggesting the possibility of monitoring homodimer/oligomer interactions between...
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08-22-2010 05:08 PM
[NMR paper] Quantitative analysis of 1H NMR detected proteins in the rat cerebral cortex in vivo
Quantitative analysis of 1H NMR detected proteins in the rat cerebral cortex in vivo and in vitro.
Related Articles Quantitative analysis of 1H NMR detected proteins in the rat cerebral cortex in vivo and in vitro.
NMR Biomed. 1993 Jul-Aug;6(4):242-7
Authors: Kauppinen RA, Niskanen T, Hakumäki J, Williams SR
Spectral editing experiments were used to quantify CH3 groups from macromolecular species in the chemical shift region from 1.2 to 1.4 ppm of rat cerebrum in vivo. Two peaks centred at 1.22 and 1.40 ppm were revealed when irradiation was...
Quantitative Study of the Oligomerization of YeastPrion Sup35NM Proteins
Linear Mode
