Literature DB >> 9887297

A method for determining B1 field inhomogeneity. Are the biases assumed in heteronuclear relaxation experiments usually underestimated?

M Guenneugues1, P Berthault, H Desvaux.   

Abstract

We describe a method allowing the determination of the effective B1 field amplitude distribution in a high-resolution NMR spectrometer. This method which can be adapted to almost any sequence, essentially consists of a mutation followed by a purging B0 gradient pulse. Experimental results obtained with this approach are described in homonuclear and heteronuclear cases. The experimental distributions are used to estimate the biases induced by B1 inhomogeneity, as well as the loss of RF power on heteronuclear transverse self-relaxation rate determination. In this type of measurement, the experimental biases induced on the intensities can be as large as 5% for long mixing times. Copyright 1999 Academic Press.

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Year:  1999        PMID: 9887297     DOI: 10.1006/jmre.1998.1590

Source DB:  PubMed          Journal:  J Magn Reson        ISSN: 1090-7807            Impact factor:   2.229


  21 in total

1.  Off-resonance effects in 15N T2 CPMG measurements.

Authors:  D M Korzhnev; E V Tischenko; A S Arseniev
Journal:  J Biomol NMR       Date:  2000-07       Impact factor: 2.835

2.  Off-resonance R1rho relaxation outside of the fast exchange limit: an experimental study of a cavity mutant of T4 lysozyme.

Authors:  Dmitry M Korzhnev; Vladislav Yu Orekhov; Frederick W Dahlquist; Lewis E Kay
Journal:  J Biomol NMR       Date:  2003-05       Impact factor: 2.835

3.  A 2D ¹³C-CEST experiment for studying slowly exchanging protein systems using methyl probes: an application to protein folding.

Authors:  Guillaume Bouvignies; Lewis E Kay
Journal:  J Biomol NMR       Date:  2012-06-12       Impact factor: 2.835

4.  Direct determination of the heteronuclear T1/T2 ratio by off-resonance steady-state magnetization measurement: Investigation of the possible application to fast exchange characterization of 15N-labeled proteins.

Authors:  M Guenneugues; P Berthault; H Desvaux; M Goldman
Journal:  J Biomol NMR       Date:  1999-12       Impact factor: 2.835

5.  (13)CHD2-CEST NMR spectroscopy provides an avenue for studies of conformational exchange in high molecular weight proteins.

Authors:  Enrico Rennella; Rui Huang; Algirdas Velyvis; Lewis E Kay
Journal:  J Biomol NMR       Date:  2015-08-14       Impact factor: 2.835

6.  Intrinsic dynamics of the partly unstructured PX domain from the Sendai virus RNA polymerase cofactor P.

Authors:  Klaartje Houben; Laurence Blanchard; Martin Blackledge; Dominique Marion
Journal:  Biophys J       Date:  2007-06-22       Impact factor: 4.033

7.  Practical considerations for investigation of protein conformational dynamics by 15N R relaxation dispersion.

Authors:  Erik Walinda; Daichi Morimoto; Masahiro Shirakawa; Kenji Sugase
Journal:  J Biomol NMR       Date:  2017-02-28       Impact factor: 2.835

8.  Probing slowly exchanging protein systems via ¹³Cα-CEST: monitoring folding of the Im7 protein.

Authors:  Alexandar L Hansen; Guillaume Bouvignies; Lewis E Kay
Journal:  J Biomol NMR       Date:  2013-02-06       Impact factor: 2.835

9.  Microsecond timescale backbone conformational dynamics in ubiquitin studied with NMR R1rho relaxation experiments.

Authors:  Francesca Massi; Michael J Grey; Arthur G Palmer
Journal:  Protein Sci       Date:  2005-03       Impact factor: 6.725

10.  Error estimation and global fitting in transverse-relaxation dispersion experiments to determine chemical-exchange parameters.

Authors:  Rieko Ishima; Dennis A Torchia
Journal:  J Biomol NMR       Date:  2005-05       Impact factor: 2.835

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