Hydrolysis of protein samples into amino acids facilitates the use of NMR spectroscopy for protein and peptide quantification. Different conditions have been tested for quantifying aromatic amino acids and proteins. The pH-dependent signal shifts in the aromatic region of amino acid samples were examined. A pH of 12 was found to minimize signal overlap of the four aromatic amino acids. Several aromatic compounds, such as terephthalic acid, sulfoisophthalic acid, and benzene tricarboxylic acid,...
[NMR analysis blog] A Novel qNMR Technique: Quantitative Global Spectrum Deconvolution (qGSD)
A Novel qNMR Technique: Quantitative Global Spectrum Deconvolution (qGSD)
Ever since chemists meddled (successfully) into NMR, with the pioneer work made by Proctor and Yu more than 67 years ago, it was implicitly used as a quantitative technique. Indeed, from the very early days of NMR, it was found that the intensity (or area) of the NMR signals (under proper operating conditions) was proportional to the number of nuclides contributing to it. Already in 1953, Jarrett, Sadler, and Shoolery showed the excellent precision of NMR (CW at that time) for the quantitative analysis of a...
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10-14-2017 04:33 PM
[NMR paper] Fluorinated Aromatic Amino Acids are Sensitive 19F NMR Probes for Bromodomain-Ligand Interactions.
Fluorinated Aromatic Amino Acids are Sensitive 19F NMR Probes for Bromodomain-Ligand Interactions.
Related Articles Fluorinated Aromatic Amino Acids are Sensitive 19F NMR Probes for Bromodomain-Ligand Interactions.
ACS Chem Biol. 2014 Oct 7;
Authors: Mishra NK, Urick AK, Ember S, Schonbrunn E, Pomerantz WC
Abstract
We describe a 19F NMR method for detecting bromodomain-ligand interactions using fluorine-labeled aromatic amino acids due to the conservation of aromatic residues in the bromodomain binding site. We test the...
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10-08-2014 05:52 PM
[NMR paper] Resonance assignment for a particularly challenging protein based on systematic unlabeling of amino acids to complement incomplete NMR data sets.
Resonance assignment for a particularly challenging protein based on systematic unlabeling of amino acids to complement incomplete NMR data sets.
Resonance assignment for a particularly challenging protein based on systematic unlabeling of amino acids to complement incomplete NMR data sets.
J Biomol NMR. 2013 Aug 14;
Authors: Bellstedt P, Seiboth T, Häfner S, Kutscha H, Ramachandran R, Görlach M
Abstract
NMR-based structure determination of a protein requires the assignment of resonances as indispensable first step. Even though...
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08-15-2013 07:45 PM
[NMR paper] Assigning the NMR spectra of aromatic amino acids in proteins: analysis of two Ets po
Assigning the NMR spectra of aromatic amino acids in proteins: analysis of two Ets pointed domains.
Related Articles Assigning the NMR spectra of aromatic amino acids in proteins: analysis of two Ets pointed domains.
Biochem Cell Biol. 1998;76(2-3):379-90
Authors: Slupsky CM, Gentile LN, McIntosh LP
The measurement of interproton nuclear Overhauser enhancements (NOEs) and dihedral angle restraints of aromatic amino acids is a critical step towards determining the structure of a protein. The complete assignment of the resonances from aromatic...
Quantitative 1H Nuclear Magnetic Resonance (qNMR) of Aromatic Amino Acids for Protein Quantification
Linear Mode
