Related ArticlesAnalysis of biological fluids using 600 MHz proton NMR spectroscopy: application of homonuclear two-dimensional J-resolved spectroscopy to urine and blood plasma for spectral simplification and assignment.
The application of 600 MHz two-dimensional J-resolved 1H NMR spectroscopy (JRES) to the analysis of human urine and blood plasma is demonstrated. This method when applied at very high field gives a rapid means of simplifying and aiding the assignment of highly overlapped resonances of minor metabolites in biofluids. Using this approach, mixtures of drug and endogenous metabolites were identified in untreated urine samples, the signals of which were extensively overlapped in single pulse 600 MHz spectra. For untreated blood plasma samples the JRES experiment was also effective for the selective attenuation of signals from the plasma proteins thus revealing strong well-resolved signals from the low molecular weight components. For the first time it was shown to be possible to assign in detail the spectra region from 3 to 4 ppm in blood plasma, including the complete assignment of the signals from alpha- and beta-glucose. JRES spectra of plasma were much easier to interpret and had a much higher information content than equivalent one-dimensional Hahn spin-echo spectra, thus aiding the identification of non protein-bound low molecular weight metabolites in plasma.
Optimization of NMR spectroscopy of encapsulated proteins dissolved in low viscosity fluids
Optimization of NMR spectroscopy of encapsulated proteins dissolved in low viscosity fluids
Abstract Comprehensive application of solution NMR spectroscopy to studies of macromolecules remains fundamentally limited by the molecular rotational correlation time. For proteins, molecules larger than 30 kDa require complex experimental methods, such as TROSY in conjunction with isotopic labeling schemes that are often expensive and generally reduce the potential information available. We have developed the reverse micelle encapsulation strategy as an alternative approach. Encapsulation of...
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07-15-2011 09:10 PM
Optimization of NMR spectroscopy of encapsulated proteins dissolved in low viscosity fluids.
Optimization of NMR spectroscopy of encapsulated proteins dissolved in low viscosity fluids.
Optimization of NMR spectroscopy of encapsulated proteins dissolved in low viscosity fluids.
J Biomol NMR. 2011 Jul 12;
Authors: Nucci NV, Marques BS, Bédard S, Dogan J, Gledhill JM, Moorman VR, Peterson RW, Valentine KG, Wand AL, Wand AJ
Comprehensive application of solution NMR spectroscopy to studies of macromolecules remains fundamentally limited by the molecular rotational correlation time. For proteins, molecules larger than 30*kDa require complex...
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07-13-2011 06:42 PM
Measurement of multiple torsional angles from one-dimensional solid-state NMR spectra: application to the conformational analysis of a ligand in its biological receptor site.
Measurement of multiple torsional angles from one-dimensional solid-state NMR spectra: application to the conformational analysis of a ligand in its biological receptor site.
Measurement of multiple torsional angles from one-dimensional solid-state NMR spectra: application to the conformational analysis of a ligand in its biological receptor site.
Phys Chem Chem Phys. 2010 Nov 14;12(42):13999-4008
Authors: Edwards R, Madine J, Fielding L, Middleton DA
Knowledge of the three-dimensional structure of a ligand in the binding site of its biological...
[NMR paper] Novel surfactant mixtures for NMR spectroscopy of encapsulated proteins dissolved in low-viscosity fluids.
Novel surfactant mixtures for NMR spectroscopy of encapsulated proteins dissolved in low-viscosity fluids.
Related Articles Novel surfactant mixtures for NMR spectroscopy of encapsulated proteins dissolved in low-viscosity fluids.
Protein Sci. 2005 Nov;14(11):2919-21
Authors: Peterson RW, Pometun MS, Shi Z, Wand AJ
NMR spectroscopy of encapsulated proteins dissolved in low-viscosity fluids is emerging as a tool for biophysical studies of proteins in atomic detail in a variety of otherwise inaccessible contexts. The central element of the...
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12-01-2010 06:56 PM
Application of NMR Spectroscopy in Medicinal Chemistry and Drug Discovery.
Application of NMR Spectroscopy in Medicinal Chemistry and Drug Discovery.
Related Articles Application of NMR Spectroscopy in Medicinal Chemistry and Drug Discovery.
Curr Top Med Chem. 2010 Sep 2;
Authors: Ohno A, Inomata K, Tochio H, Shirakawa M
"In-cell nuclear magnetic resonance (NMR)" is a unique method for characterization of conformation, interaction and dynamics of proteins inside living cells at atomic level. Since the method was proposed by Dötch and co-workers in 2001 , its application had been limited to bacterial cells and...
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09-03-2010 02:30 PM
[NMR paper] Analysis of a peptide inhibitor of paramyxovirus (NDV) fusion using biological assays
Analysis of a peptide inhibitor of paramyxovirus (NDV) fusion using biological assays, NMR, and molecular modeling.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Analysis of a peptide inhibitor of paramyxovirus (NDV) fusion using biological assays, NMR, and molecular modeling.
Virology. 1997 Nov 24;238(2):291-304
Authors: Young JK, Hicks RP, Wright GE, Morrison TG
To investigate the molecular mechanisms involved in paramyxovirus-induced cell fusion, the function and...
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08-22-2010 05:08 PM
NMRFAM Workshop: NMR data collection and analysis for biological structure determination
NMRFAM Workshop: NMR data collection and analysis for biological structure determination
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The NMR facility is pleased to announce its first NMRFAM workshop to be held from noon June 6 through noon June 9, 2006 in the Biochemistry Addition at the University of Wisconsin-Madison.
The detailed program for the workshop is now available.
Purpose This workshop will offer a unique opportunity for participants to experience a combination of hands-on computational sessions, presentations, and discussions focusing on recently developed tools as well as emerging methods in NMR data...