Quantifying the amounts and types of lipids present in mixtures is important in fields as diverse as medicine, food science, and biochemistry. Nuclear magnetic resonance (NMR) spectroscopy can quantify the total amounts of saturated and unsaturated fatty acids in mixtures, but identifying the length of saturated fatty acid or the position of unsaturation by NMR is a daunting challenge. We have developed an NMR technique, aliphatic chain length by isotropic mixing, to address this problem. Using a selective total correlation spectroscopy technique to excite and transfer magnetization from a resolved resonance, we demonstrate that the time dependence of this transfer to another resolved site depends linearly on the number of aliphatic carbons separating the two sites. This technique is applied to complex natural mixtures allowing the identification and quantification of the constituent fatty acids. The method has been applied to whole adipocytes demonstrating that it will be of great use in studies of whole tissues.
[NMR paper] Solid-state NMR studies of full-length BamA in lipid bilayers suggest limited overall POTRA mobility.
Solid-state NMR studies of full-length BamA in lipid bilayers suggest limited overall POTRA mobility.
Related Articles Solid-state NMR studies of full-length BamA in lipid bilayers suggest limited overall POTRA mobility.
J Mol Biol. 2014 Feb 12;
Authors: Sinnige T, Weingarth M, Renault M, Baker L, Tommassen J, Baldus M
Abstract
The outer membrane protein BamA is the key player in ?-barrel assembly in Gram-negative bacteria. Despite the availability of high-resolution crystal structures, the dynamic behavior of the transmembrane domain and...
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02-19-2014 12:07 AM
[NMR paper] Solution NMR assignment of the heavy chain complex of the human cardiac myosin regulatory light chain.
Solution NMR assignment of the heavy chain complex of the human cardiac myosin regulatory light chain.
Related Articles Solution NMR assignment of the heavy chain complex of the human cardiac myosin regulatory light chain.
Biomol NMR Assign. 2014 Jan 12;
Authors: Rostkova E, Gautel M, Pfuhl M
Abstract
The regulatory light chain (RLC) of striated and cardiac muscle myosin plays a complex role in muscle function and regulation. Together with the essential light chain it provides stability to the lever arm, which is essential for force...
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01-15-2014 05:16 PM
[NMR paper] Improved NMR experiments with (13)C-isotropic mixing for assignment of aromatic and aliphatic side chains in labeled proteins.
Improved NMR experiments with (13)C-isotropic mixing for assignment of aromatic and aliphatic side chains in labeled proteins.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Improved NMR experiments with (13)C-isotropic mixing for assignment of aromatic and aliphatic side chains in labeled proteins.
J Biomol NMR. 2014 Jan 4;
Authors: Kovacs H, Gossert A
Abstract
Three improved (13)C-spinlock experiments for side chain assignments of...
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01-07-2014 11:16 PM
[Question from NMRWiki Q&A forum] How to calibrate pulse length for urine samples?
How to calibrate pulse length for urine samples?
I recently read an article about executing a WET sequence for water suppression in urine samples. The 90°excitation pulse should be calibrated at the beginning of the data acquisition for each sample. what causes the changes of pulse length between different samples? I've read the book "200 and more nmr experiments" and other manuals but I couldn't find the answer. I'm confused about how to selected a proper resonance in mixture for calibration. Should I choose the water resonance in urine spectra for calibraion? Because other signals were...
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12-18-2013 03:14 AM
[NMR paper] Lipid bilayer preparations of membrane proteins for oriented and magic-angle spinning solid-state NMR samples.
Lipid bilayer preparations of membrane proteins for oriented and magic-angle spinning solid-state NMR samples.
Related Articles Lipid bilayer preparations of membrane proteins for oriented and magic-angle spinning solid-state NMR samples.
Nat Protoc. 2013 Nov;8(11):2256-70
Authors: Das N, Murray DT, Cross TA
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10-27-2013 12:53 AM
[Question from NMRWiki Q&A forum] Longer pulse length for conducting samples?
Longer pulse length for conducting samples?
Hi, my 1H 90 deg pulses are always longer when I work with my samples that are electrically conducting. Is this a/the reason why it is long? Any similar experiences?
Check if somebody has answered this question on NMRWiki QA forum
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08-04-2012 05:22 AM
[NMR paper] Optimizing oriented planar-supported lipid samples for solid-state protein NMR.
Optimizing oriented planar-supported lipid samples for solid-state protein NMR.
Related Articles Optimizing oriented planar-supported lipid samples for solid-state protein NMR.
Biophys J. 2005 Oct;89(4):2792-805
Authors: Rainey JK, Sykes BD
Sample orientation relative to the static magnetic field of an NMR spectrometer allows study of membrane proteins in the lipid bilayer setting. The straightforward preparation and handling of extremely thin mica substrates with consistent surface properties has prompted us to examine oriented phospholipid...
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12-01-2010 06:56 PM
[NMR paper] Mixing apparatus for preparing NMR samples under pressure.
Mixing apparatus for preparing NMR samples under pressure.
Related Articles Mixing apparatus for preparing NMR samples under pressure.
J Magn Reson. 2003 Sep;164(1):84-91
Authors: Wu WJ, Vidugiris G, Mooberry ES, Westler WM, Markley JL
The size limit for protein NMR spectroscopy in solution arises in large part from line broadening caused by slow molecular tumbling. One way to alleviate this problem is to increase the effective tumbling rate by reducing the viscosity of the solvent. Because proteins generally require an aqueous environment to...
Aliphatic chain length by isotropic mixing (ALCHIM): determining composition of complex lipid samples by 1H NMR spectroscopy
Linear Mode
