Related ArticlesThe IR-(15)N-HSQC-AP experiment: a new tool for NMR spectroscopy of paramagnetic molecules.
J Biomol NMR. 2014 Jan 11;
Authors: Ciofi-Baffoni S, Gallo A, Muzzioli R, Piccioli M
Abstract
A crucial factor for the understanding of structure-function relationships in metalloproteins is the identification of NMR signals from residues surrounding the metal cofactor. When the latter is paramagnetic, the NMR information in the proximity of the metal center may be scarce, because fast nuclear relaxation quenches signal intensity and coherence transfer efficiency. To identify residues at a short distance from a paramagnetic center, we developed a modified version of the (15)N-HSQC experiment where (1) an inversion recovery filter is added prior to HSQC, (2) the INEPT period has been optimized according to fast relaxation of interested spins, (3) the inverse INEPT has been eliminated and signals acquired as antiphase doublets. The experiment has been successfully tested on a human [Fe2S2] protein which is involved in the biogenesis of iron-sulfur proteins. Thirteen HN resonances, unobserved with conventional HSQC experiments, could be identified. The structural arrangement of the protein scaffold in the proximity of the Fe/S cluster is fundamental to comprehend the molecular processes responsible for the transfer of Fe/S groups in the iron-sulfur protein assembly machineries.
PMID: 24414179 [PubMed - as supplied by publisher]
1H-15N HSQC, edited by a 1H inversion recovery and observed in the antiphase component (IR-HSQC-AP)
Could someone explain the experimental theory/basis behind 1H-15N inversion recovery filtered HSQC experiment observed in antiphase (IR-HSQC-AP)? I am still learning basic NMR theory, but would like to know about this particular experiment, which was used to detect paramagnetically broadened backbone resonances. Thanks.
Abstract
Biogenesis of iron–sulfur cluster proteins is a highly regulated process that requires complex protein machineries. In the cytosolic iron–sulfur protein assembly machinery, two human key proteins—NADPH-dependent diflavin oxidoreductase 1 (Ndor1) and...
[NMR paper] Keeping PASE with WEFT: SHWEFT-PASE pulse sequences for (1) H NMR spectra of highly paramagnetic molecules.
Keeping PASE with WEFT: SHWEFT-PASE pulse sequences for (1) H NMR spectra of highly paramagnetic molecules.
Related Articles Keeping PASE with WEFT: SHWEFT-PASE pulse sequences for (1) H NMR spectra of highly paramagnetic molecules.
Magn Reson Chem. 2013 Feb 10;
Authors: Helms G, Satterlee JD
Abstract
Metalloproteins are a category of biomolecules in which the metal site is usually the locus of activity or function. In many cases, the metal ions are paramagnetic or have accessible paramagnetic states, many of which can be studied using NMR...
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02-13-2013 12:47 PM
[NMR paper] Measuring protein reduction potentials using (15)N HSQC NMR spectroscopy.
Measuring protein reduction potentials using (15)N HSQC NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.rsc.org-images-entities-char_z_RSClogo.gif Related Articles Measuring protein reduction potentials using (15)N HSQC NMR spectroscopy.
Chem Commun (Camb). 2013 Jan 29;
Authors: Taylor SL, Crawley-Snowdon H, Wagstaff JL, Rowe ML, Shepherd M, Williamson RA, Howard MJ
Abstract
NMR spectroscopy was used to measure reduction potentials of four redox proteins by following multiple (15)N HSQC protein resonances...
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02-03-2013 10:19 AM
[Question from NMRWiki Q&A forum] why we are seeing negative PREs in paramagnetic relaxation enhancement experiment?
why we are seeing negative PREs in paramagnetic relaxation enhancement experiment?
Hi NMR Wiki users,
I'm using two point method(Marius Clore and Junji Iwahara methods) to measure the PREs, but in my experiment I observed so many negative PREs. Is there any chance to use these negative PREs data in structure calculation.How can I get all positive PREs,otherwise I lose half of the data in my calculations.
Check if somebody has answered this question on NMRWiki QA forum
The IR-(15)N-HSQC-AP experiment: a new tool for NMR spectroscopy of paramagnetic molecules.
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