Related ArticlesUTOPIA NMR: activating unexploited magnetization using interleaved low-gamma detection.
J Biomol NMR. 2016 Jan 4;
Authors: Viegas A, Viennet T, Yu TY, Schumann F, Bermel W, Wagner G, Etzkorn M
Abstract
A growing number of nuclear magnetic resonance (NMR) spectroscopic studies are impaired by the limited information content provided by the standard set of experiments conventionally recorded. This is particularly true for studies of challenging biological systems including large, unstructured, membrane-embedded and/or paramagnetic proteins. Here we introduce the concept of unified time-optimized interleaved acquisition NMR (UTOPIA-NMR) for the unified acquisition of standard high-? (e.g. (1)H) and low-? (e.g. (13)C) detected experiments using a single receiver. Our aim is to activate the high level of polarization and information content distributed on low-? nuclei without disturbing conventional magnetization transfer pathways. We show that using UTOPIA-NMR we are able to recover nearly all of the normally non-used magnetization without disturbing the standard experiments. In other words, additional spectra, that can significantly increase the NMR insights, are obtained for free. While we anticipate a broad range of possible applications we demonstrate for the soluble protein Bcl-xL (ca. 21*kDa) and for OmpX in nanodiscs (ca. 160*kDa) that UTOPIA-NMR is particularly useful for challenging protein systems including perdeuterated (membrane) proteins.
PMID: 26728075 [PubMed - as supplied by publisher]
UTOPIA NMR: activating unexploited magnetization using interleaved low-gamma detection
UTOPIA NMR: activating unexploited magnetization using interleaved low-gamma detection
Abstract
A growing number of nuclear magnetic resonance (NMR) spectroscopic studies are impaired by the limited information content provided by the standard set of experiments conventionally recorded. This is particularly true for studies of challenging biological systems including large, unstructured, membrane-embedded and/or paramagnetic proteins. Here we introduce the concept of unified time-optimized interleaved acquisition NMR (UTOPIA-NMR) for the unified...
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01-04-2016 07:49 PM
[NMR paper] Nmr structural studies of the first catalytic half-domain of ubiquitin activating enzyme.
Nmr structural studies of the first catalytic half-domain of ubiquitin activating enzyme.
Related Articles Nmr structural studies of the first catalytic half-domain of ubiquitin activating enzyme.
J Struct Biol. 2013 Nov 6;
Authors: Jaremko M, Jaremko L, Nowakowski M, Wojciechowski M, Szczepanowski RH, Panecka R, Zhukov I, Bochtler M, Ejchart A
Abstract
We report a high resolution NMR structure and (15)N relaxation studies of the first catalytic cysteine half-domain (FCCH) of the mouse ubiquitin-activating enzyme E1, together with...
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11-12-2013 03:52 PM
[NMRpipe Yahoo group] script for processing interleaved 3D experiment
script for processing interleaved 3D experiment
Hello NMRPipe Community, I have a 3D data set (modified HNCO experiment for detection of Hydrogen bonding partners) wherein the reference and the H-bond
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05-15-2013 03:12 PM
[NMRpipe Yahoo group] script for processing interleaved 3D experiment
script for processing interleaved 3D experiment
Hello NMRPipe Community, I have a 3D data set (modified HNCO experiment for detection of Hydrogen bonding partners) wherein the reference and the H-bond
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05-06-2013 11:24 AM
[NMRpipe Yahoo group] Re: Processing interleaved pseudo 3D Bruker data
Re: Processing interleaved pseudo 3D Bruker data
Hi All ... Sorry I didn't write sooner. I moved from the DC area to the West Coast this week. Find me in the happy town of Campbell CA, the reputed
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06-17-2012 11:32 PM
NMR Solution Structure of a Photoswitchable Apoptosis Activating Bak Peptide Bound to Bcl-xL
NMR Solution Structure of a Photoswitchable Apoptosis Activating Bak Peptide Bound to Bcl-xL
Piotr Wysoczanski, Robert J. Mart, E. Joel Loveridge, Christopher Williams, Sara B.-M. Whittaker, Matthew P. Crump and Rudolf K. Allemann
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja302390a/aop/images/medium/ja-2012-02390a_0003.gif
Journal of the American Chemical Society
DOI: 10.1021/ja302390a
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/OkkweMR_zn8
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04-26-2012 06:28 AM
NMR assignments of ubiquitin fold domain (UFD) in SUMO-activating enzyme subunit 2 from rice.
NMR assignments of ubiquitin fold domain (UFD) in SUMO-activating enzyme subunit 2 from rice.
NMR assignments of ubiquitin fold domain (UFD) in SUMO-activating enzyme subunit 2 from rice.
Biomol NMR Assign. 2011 Apr 27;
Authors: Suzuki R, Tsuchiya W, Shindo H, Yamazaki T
The small ubiquitin-related modifier (SUMO) is a ubiquitin-like post-translational modifier that alters the localization, activity, or stability of many proteins. In the sumoylation process, an activated SUMO is transferred from SUMO-activating enzyme E1 complex (SAE1/SAE2) to...
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04-28-2011 03:12 PM
[NMR paper] NMR structure and dynamics of monomeric neutrophil-activating peptide 2.
NMR structure and dynamics of monomeric neutrophil-activating peptide 2.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.biochemj.org-images-bj_pubmed.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles NMR structure and dynamics of monomeric neutrophil-activating peptide 2.
Biochem J. 1999 Mar 15;338 ( Pt 3):591-8
Authors: Young H, Roongta V, Daly TJ, Mayo KH
Neutrophil-activating peptide 2 (NAP-2), which demonstrates a range of proinflammatory...