Combinatorial triple-selective labeling as a tool to assist membrane protein backbone resonance assignment
Combinatorial triple-selective labeling as a tool to assist membrane protein backbone resonance assignment
Abstract Obtaining NMR assignments for slowly tumbling molecules such as detergent-solubilized membrane proteins is often compromised by low sensitivity as well as spectral overlap. Both problems can be addressed by amino-acid specific isotope labeling in conjunction with 15Nā??1H correlation experiments. In this work an extended combinatorial selective in vitro labeling scheme is proposed that seeks to reduce the number of samples required for assignment. Including three...
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01-21-2012 06:26 PM
Frequency-selective heteronuclear dephasing and selective carbonyl labeling to deconvolute crowded spectra of membrane proteins by magic angle spinning NMR.
Frequency-selective heteronuclear dephasing and selective carbonyl labeling to deconvolute crowded spectra of membrane proteins by magic angle spinning NMR.
Frequency-selective heteronuclear dephasing and selective carbonyl labeling to deconvolute crowded spectra of membrane proteins by magic angle spinning NMR.
J Magn Reson. 2011 Mar 17;
Authors: Traaseth NJ, Veglia G
We present a new method that combines carbonyl-selective labeling with frequency-selective heteronuclear recoupling to resolve the spectral overlap of magic angle spinning (MAS) NMR...
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04-13-2011 11:57 PM
Frequency-Selective Heteronuclear Dephasing and Selective Carbonyl Labeling to Deconvolute Crowded Spectra of Membrane Proteins By Magic Angle Spinning NMR
Frequency-Selective Heteronuclear Dephasing and Selective Carbonyl Labeling to Deconvolute Crowded Spectra of Membrane Proteins By Magic Angle Spinning NMR
Publication year: 2011
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 17 March 2011</br>
Nathaniel J., Traaseth , Gianluigi, Veglia</br>
We present a new method that combines carbonyl-selective labeling with frequency-selective heteronuclear recoupling to resolve the spectral overlap of magic angle spinning (MAS) NMR spectra of membrane proteins in fluid lipid membranes with broad lines and...
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03-18-2011 06:43 AM
[NMR paper] Use of selective Trp side chain labeling to characterize protein-protein and protein-
Use of selective Trp side chain labeling to characterize protein-protein and protein-ligand interactions by NMR spectroscopy.
Related Articles Use of selective Trp side chain labeling to characterize protein-protein and protein-ligand interactions by NMR spectroscopy.
J Am Chem Soc. 2003 Mar 12;125(10):2892-3
Authors: Rodriguez-Mias RA, Pellecchia M
Recent studies on amino acid occurrence in protein binding sites suggest that only a reduced number of residues are responsible for most interaction energy in protein-protein and protein-ligand...
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11-24-2010 09:01 PM
[NMR paper] Protein expression, selective isotopic labeling, and analysis of hyperfine-shifted NM
Protein expression, selective isotopic labeling, and analysis of hyperfine-shifted NMR signals of Anabaena 7120 vegetative ferredoxin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Protein expression, selective isotopic labeling, and analysis of hyperfine-shifted NMR signals of Anabaena 7120 vegetative ferredoxin.
Arch Biochem Biophys. 1995 Jan 10;316(1):619-34
Authors: Cheng H, Westler WM, Xia B, Oh BH, Markley JL
Two alternative T7 RNA promoter/polymerase systems...
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08-22-2010 03:41 AM
[NMR paper] URPI: a utility program for planning selective protein double-labeling with 13C and 1
URPI: a utility program for planning selective protein double-labeling with 13C and 15N in NMR analyses.
Related Articles URPI: a utility program for planning selective protein double-labeling with 13C and 15N in NMR analyses.
J Magn Reson B. 1994 Jan;103(1):89-90
Authors: Shinagawa K, Ohya M, Wakamatsu K
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08-22-2010 03:33 AM
[NMR paper] Selective and extensive 13C labeling of a membrane protein for solid-state NMR invest
Selective and extensive 13C labeling of a membrane protein for solid-state NMR investigations.
Related Articles Selective and extensive 13C labeling of a membrane protein for solid-state NMR investigations.
J Biomol NMR. 1999 May;14(1):71-4
Authors: Hong M, Jakes K
The selective and extensive 13C labeling of mostly hydrophobic amino acid residues in a 25 kDa membrane protein, the colicin Ia channel domain, is reported. The novel 13C labeling approach takes advantage of the amino acid biosynthetic pathways in bacteria and suppresses the...
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08-21-2010 04:03 PM
Investigation of the utility of selective methyl protonation for determination of membrane protein structures
Investigation of the utility of selective methyl protonation for determination of membrane protein structures
Steve C. C. Shih, Ileana Stoica and Natalie K. Goto
Journal of Biomolecular NMR; 2008; 42(1); pp 49-58
Abstract
Polytopic α-helical membrane proteins present one of the final frontiers for protein structural biology, with significant challenges causing severe under-representation in the protein structure databank. However, with the advent of hardware and methodology geared to the study of large molecular weight complexes, solution NMR is being increasingly considered as a tool...
URPI: a utility program for planning selective protein double-labeling with 13C and 1
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