Real-time pure shift 15 N HSQC of proteins: a real improvement in resolution and sensitivity
Real-time pure shift 15 N HSQC of proteins: a real improvement in resolution and sensitivity
Abstract
Spectral resolution in proton NMR spectroscopy is reduced by the splitting of resonances into multiplets due to the effect of homonuclear scalar couplings. Although these effects are often hidden in protein NMR spectroscopy by low digital resolution and routine apodization, behind the scenes homonuclear scalar couplings increase spectral overcrowding. The possibilities for biomolecular NMR offered by new pure shift NMR methods are illustrated here....
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03-04-2015 08:56 AM
[NMR paper] Detection of a transient intramolecular hydrogen bond using 1JNH scalar couplings
Detection of a transient intramolecular hydrogen bond using 1JNH scalar couplings
Publication date: Available online 18 April 2014
Source:Journal of Magnetic Resonance</br>
Author(s): ShengQi Xiang , Markus Zweckstetter</br>
Hydrogen bonds are essential for the structure, stability and folding of proteins. The identification of intramolecular hydrogen bonds, however, is challenging, in particular in transiently folded states. Here we studied the presence of intramolecular hydrogen bonds in the folding nucleus of the coiled-coil structure of the GCN4 leucine zipper....
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04-18-2014 01:35 PM
[NMR paper] A Computational Study of the Effects of (13) C-(13) C Scalar Couplings on (13) C CEST NMR Spectra: Towards Studies on a Uniformly (13) C-Labeled Protein.
A Computational Study of the Effects of (13) C-(13) C Scalar Couplings on (13) C CEST NMR Spectra: Towards Studies on a Uniformly (13) C-Labeled Protein.
A Computational Study of the Effects of (13) C-(13) C Scalar Couplings on (13) C CEST NMR Spectra: Towards Studies on a Uniformly (13) C-Labeled Protein.
Chembiochem. 2013 Jun 19;
Authors: Vallurupalli P, Bouvignies G, Kay LE
Abstract
Read the label: The NMR CEST experiment can be used to reconstruct spectra of sparsely populated, transiently formed protein conformers so long as...
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06-21-2013 01:10 PM
[NMR paper] Protein folding studied by real-time NMR spectroscopy.
Protein folding studied by real-time NMR spectroscopy.
Related Articles Protein folding studied by real-time NMR spectroscopy.
Methods. 2004 Sep;34(1):65-74
Authors: Zeeb M, Balbach J
Real-time NMR spectroscopy developed to a generally applicable method to follow protein folding reactions. It combines the access to high resolution data with kinetic experiments allowing very detailed insights into the development of the protein structure during different steps of folding. The present review concentrates mainly on the progress of real-time NMR...
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11-24-2010 10:01 PM
[NMR paper] NMR scalar couplings across Watson-Crick base pair hydrogen bonds in DNA observed by
NMR scalar couplings across Watson-Crick base pair hydrogen bonds in DNA observed by transverse relaxation-optimized spectroscopy.
Related Articles NMR scalar couplings across Watson-Crick base pair hydrogen bonds in DNA observed by transverse relaxation-optimized spectroscopy.
Proc Natl Acad Sci U S A. 1998 Nov 24;95(24):14147-51
Authors: Pervushin K, Ono A, Fernández C, Szyperski T, Kainosho M, Wüthrich K
This paper describes the NMR observation of 15N---15N and 1H---15N scalar couplings across the hydrogen bonds in Watson-Crick base pairs...
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11-17-2010 11:15 PM
[NMR paper] Following protein folding in real time using NMR spectroscopy.
Following protein folding in real time using NMR spectroscopy.
Related Articles Following protein folding in real time using NMR spectroscopy.
Nat Struct Biol. 1995 Oct;2(10):865-70
Authors: Balbach J, Forge V, van Nuland NA, Winder SL, Hore PJ, Dobson CM
The refolding of apo bovine alpha-lactalbumin has been monitored in real time by NMR spectroscopy following rapid in situ dilution of a chemically denatured state. By examining individual resonances in the time-resolved NMR spectra, the native state has been shown to emerge in a cooperative...
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08-22-2010 03:50 AM
MQ-HNCO-TROSY for the measurement of scalar and residual dipolar couplings in larger
Abstract We describe a novel pulse sequence, MQ-HNCO-TROSY, for the measurement of scalar and residual dipolar couplings between amide proton and nitrogen in larger proteins. The experiment utilizes the whole 2TN polarization transfer delay for labeling of 15N chemical shift in a constant time manner, which efficiently doubles the attainable resolution in 15N dimension with respect to the conventional HNCO-TROSY experiment. In addition, the accordion principle is employed for measuring (J + D)NHs, and the multiplet components are selected with the generalized version of the TROSY scheme...
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08-14-2010 04:19 AM
S3EPY: a Sparky extension for determination of small scalar couplings from spin-state
Abstract S3EPY is a Python extension to the program Sparky written to facilitate the assessment of coupling constants from in-phase/antiphase and spin-state-selective excitation (S3E) experiments. It enables the routine use of small scalar couplings by automating the coupling evaluation procedure. S3EPY provides an integrated graphical user interface to programs which outputs graphs and the table of determined couplings.
Content Type Journal Article
DOI 10.1007/s10858-009-9392-1
Authors
Petr Novák, Masaryk University National Centre for Biomolecular Research, Faculty of Science...
VisualizingUnresolved Scalar Couplings by Real-Time J-UpscaledNMR
Linear Mode
