Related ArticlesSpin-state-selective TPPI: a new method for suppression of heteronuclear coupling constants in multidimensional NMR experiments.
J Magn Reson. 1999 Aug;139(2):443-6
Authors: Schulte-Herbrüggen T, Briand J, Meissner A, Sřrensen OW
A novel multidimensional NMR pulse sequence tool, spin-state-selective time-proportional phase incrementation (S(3) TPPI), is introduced. It amounts to application of different TPPIs on the two components of doublets so that their frequencies can be manipulated independently. The chief application is for suppression of large heteronuclear one-bond coupling constants in indirect dimensions of multidimensional experiments without interchanging the two transverse magnetization components of doublets as conventional decoupling does, which is advantageous when they relax at different rates such as by partial compensation of dipolar and CSA relaxation contributions. For experimental confirmation we use a sample of (15)N-labeled neural cell adhesion molecule modules 1 and 2, a protein with a molecular weight of about 20 kDa. The new tool is general and can be combined with many multidimensional NMR experiments for proteins.
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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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
Suppression of isotope scrambling in cell-free protein synthesis by broadband inhibition of PLP enymes for selective 15N-labelling and production of perdeuterated proteins in H2O
Suppression of isotope scrambling in cell-free protein synthesis by broadband inhibition of PLP enymes for selective 15N-labelling and production of perdeuterated proteins in H2O
Abstract Selectively isotope labelled protein samples can be prepared in vivo or in vitro from selectively labelled amino acids but, in many cases, metabolic conversions between different amino acids result in isotope scrambling. The best results are obtained by cell-free protein synthesis, where metabolic enzymes are generally less active, but isotope scrambling can never be suppressed completely. We show that...
[NMR paper] Investigation of the NMR spin-spin coupling constants across the hydrogen bonds in ub
Investigation of the NMR spin-spin coupling constants across the hydrogen bonds in ubiquitin: the nature of the hydrogen bond as reflected by the coupling mechanism.
Related Articles Investigation of the NMR spin-spin coupling constants across the hydrogen bonds in ubiquitin: the nature of the hydrogen bond as reflected by the coupling mechanism.
J Am Chem Soc. 2004 Apr 28;126(16):5093-107
Authors: Tuttle T, Kraka E, Wu A, Cremer D
The indirect scalar NMR spin-spin coupling constants across the H-bonds of the protein ubiquitin were calculated,...
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[NMR paper] 19F-NMR spin-spin relaxation (T2) method for characterizing volatile anesthetic bindi
19F-NMR spin-spin relaxation (T2) method for characterizing volatile anesthetic binding to proteins. Analysis of isoflurane binding to serum albumin.
Related Articles 19F-NMR spin-spin relaxation (T2) method for characterizing volatile anesthetic binding to proteins. Analysis of isoflurane binding to serum albumin.
Biochemistry. 1992 Aug 11;31(31):7069-76
Authors: Dubois BW, Evers AS
This paper characterizes the low-affinity ligand binding interactions of a fluorinated volatile anesthetic, isoflurane (CHF2OCHClCF3), with bovine serum albumin...
Spin-state-selective TPPI: a new method for suppression of heteronuclear coupling con
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